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LongText Report for: 3PFB-pdb

Name Class
3PFB-pdb
HEADER    HYDROLASE                               28-OCT-10   3PFB              
TITLE     CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE   
TITLE    2 LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CINNAMOYL ESTERASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS JOHNSONII;                        
SOURCE   3 ORGANISM_TAXID: 33959;                                               
SOURCE   4 GENE: LJ0536;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P15TV-L                                   
KEYWDS    ALPHA/BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CINNAMOYL/FERULOYL    
KEYWDS   2 ESTERASE, HYDROXYCINAMMATES, EXTRACELLULAR                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.STOGIOS,K.K.LAI,C.VU,X.XU,H.CUI,S.MOLLOY,C.F.GONZALEZ,A.YAKUNIN,  
AUTHOR   2 A.SAVCHENKO                                                          
REVDAT   1   31-AUG-11 3PFB    0                                                
JRNL        AUTH   K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,S.MOLLOY,A.SAVCHENKO,    
JRNL        AUTH 2 A.YAKUNIN,C.F.GONZALEZ                                       
JRNL        TITL   AN INSERTED ALPHA/BETA SUBDOMAIN SHAPES THE CATALYTIC POCKET 
JRNL        TITL 2 OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE                
JRNL        REF    PLOS ONE                      V.   6       2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        DOI    10.1371/JOURNAL.PONE.0023269                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 73.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 49803                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2673                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1170                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 23.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 907                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.65000                                              
REMARK   3    B22 (A**2) : -1.61000                                             
REMARK   3    B33 (A**2) : 0.97000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.680         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4057 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5519 ; 1.933 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 6.860 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;35.660 ;25.124       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   660 ;15.050 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.668 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   621 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3140 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2498 ; 1.698 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4036 ; 2.393 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1559 ; 4.285 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1477 ; 5.708 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4057 ; 2.268 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -4        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2581  55.2849  12.7899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -4        B   329                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.5964  28.7589  31.7760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3PFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062308.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52487                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 73.1                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200   FOR THE DATA SET  : 31.2100                            
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     (%) : 21.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26000                            
REMARK 200   FOR SHELL         : 3.090                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII     
REMARK 200  CINNAMOYL ESTERASE LJ0536 S106A MUTANT                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M AMMONIUM        
REMARK 280  SULPHATE, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.13000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.94550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.13000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.94550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     ASN A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     ALA A   248                                                      
REMARK 465     PHE A   249                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B   245                                                      
REMARK 465     ASN B   246                                                      
REMARK 465     ASN B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     PHE B   249                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1693     O    HOH B  2004              2.08            
REMARK 500   O    ASP A     9     O    ASP B     9              2.10            
REMARK 500   O    HOH A  1914     O    HOH B  2072              2.13            
REMARK 500   O    HOH A   742     O    HOH A   963              2.14            
REMARK 500   O    HOH B  1440     O    HOH B  1514              2.15            
REMARK 500   O    HOH B   310     O    HOH B   403              2.16            
REMARK 500   O    HOH B   485     O    HOH B   765              2.16            
REMARK 500   OE1  GLN B   244     O    HOH B  1685              2.16            
REMARK 500   O    HOH A   624     O    HOH A  1648              2.17            
REMARK 500   OG1  THR A     3     O    HOH A  1560              2.18            
REMARK 500   CD1  LEU A   115     O    HOH A  1103              2.19            
REMARK 500   O    GLN A    -1     O    HOH A   275              2.19            
REMARK 500   ND2  ASN A    99     O    HOH A  1679              2.19            
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    LEU B 176   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 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   9       57.02     38.75                                   
REMARK 500    ARG A  98      -82.48   -100.89                                   
REMARK 500    ALA A 106     -121.19     54.65                                   
REMARK 500    ALA A 132       55.04    -91.40                                   
REMARK 500    LYS A 161     -129.36     49.52                                   
REMARK 500    ASP A 229     -120.99     54.63                                   
REMARK 500    THR B  35      -10.22     79.11                                   
REMARK 500    ARG B  98      -90.23    -94.16                                   
REMARK 500    ALA B 106     -118.90     57.64                                   
REMARK 500    ASP B 162      -15.26     83.60                                   
REMARK 500    ASP B 229     -119.06     50.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B  79        23.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 254                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 254                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 259                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 260                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 261                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 255                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYC B 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYC A 256                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536                                                      
REMARK 900 RELATED ID: 3PF9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT                                         
REMARK 900 RELATED ID: 3PFA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID            
REMARK 900 RELATED ID: 3PFC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH FERULIC ACID            
DBREF  3PFB A    1   249  UNP    D3YEX6   D3YEX6_LACJO     1    249             
DBREF  3PFB B    1   249  UNP    D3YEX6   D3YEX6_LACJO     1    249             
SEQADV 3PFB MET A  -20  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY A  -19  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER A  -18  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER A  -17  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -16  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -15  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -14  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -13  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -12  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS A  -11  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER A  -10  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER A   -9  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY A   -8  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ARG A   -7  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLU A   -6  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ASN A   -5  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB LEU A   -4  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB TYR A   -3  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB PHE A   -2  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLN A   -1  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY A    0  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ALA A  106  UNP  D3YEX6    SER   106 ENGINEERED MUTATION            
SEQADV 3PFB MET B  -20  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY B  -19  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER B  -18  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER B  -17  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -16  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -15  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -14  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -13  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -12  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB HIS B  -11  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER B  -10  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB SER B   -9  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY B   -8  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ARG B   -7  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLU B   -6  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ASN B   -5  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB LEU B   -4  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB TYR B   -3  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB PHE B   -2  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLN B   -1  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB GLY B    0  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PFB ALA B  106  UNP  D3YEX6    SER   106 ENGINEERED MUTATION            
SEQRES   1 A  270  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  270  ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR          
SEQRES   3 A  270  LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU          
SEQRES   4 A  270  GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE          
SEQRES   5 A  270  HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG          
SEQRES   6 A  270  GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER          
SEQRES   7 A  270  VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY          
SEQRES   8 A  270  LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP          
SEQRES   9 A  270  ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS          
SEQRES  10 A  270  VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY          
SEQRES  11 A  270  VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU          
SEQRES  12 A  270  ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU          
SEQRES  13 A  270  LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR          
SEQRES  14 A  270  TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS          
SEQRES  15 A  270  ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN          
SEQRES  16 A  270  GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS          
SEQRES  17 A  270  PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL          
SEQRES  18 A  270  SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN          
SEQRES  19 A  270  ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS          
SEQRES  20 A  270  PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR          
SEQRES  21 A  270  THR ASP PHE LEU GLN ASN ASN ASN ALA PHE                      
SEQRES   1 B  270  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  270  ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR          
SEQRES   3 B  270  LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU          
SEQRES   4 B  270  GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE          
SEQRES   5 B  270  HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG          
SEQRES   6 B  270  GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER          
SEQRES   7 B  270  VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY          
SEQRES   8 B  270  LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP          
SEQRES   9 B  270  ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS          
SEQRES  10 B  270  VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY          
SEQRES  11 B  270  VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU          
SEQRES  12 B  270  ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU          
SEQRES  13 B  270  LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR          
SEQRES  14 B  270  TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS          
SEQRES  15 B  270  ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN          
SEQRES  16 B  270  GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS          
SEQRES  17 B  270  PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL          
SEQRES  18 B  270  SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN          
SEQRES  19 B  270  ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS          
SEQRES  20 B  270  PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR          
SEQRES  21 B  270  THR ASP PHE LEU GLN ASN ASN ASN ALA PHE                      
HET    NH4  A 250       1                                                       
HET    NH4  A 251       1                                                       
HET    NH4  A 252       1                                                       
HET    NH4  A 253       1                                                       
HET    NH4  A 254       1                                                       
HET     CL  A 255       1                                                       
HET    ZYC  A 256      16                                                       
HET    NH4  B 250       1                                                       
HET    NH4  B 251       1                                                       
HET    NH4  B 252       1                                                       
HET    NH4  B 253       1                                                       
HET    NH4  B 254       1                                                       
HET    NH4  B 255       1                                                       
HET    NH4  B 256       1                                                       
HET    NH4  B 257       1                                                       
HET    NH4  B 258       1                                                       
HET    NH4  B 259       1                                                       
HET    NH4  B 260       1                                                       
HET     CL  B 261       1                                                       
HET     CL  B 262       1                                                       
HET     CL  B 263       1                                                       
HET    ZYC  B 264      16                                                       
HETNAM     NH4 AMMONIUM ION                                                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ZYC ETHYL (2E)-3-(4-HYDROXY-3-METHOXYPHENYL)PROP-2-ENOATE            
HETSYN     ZYC ETHYL FERULATE                                                   
FORMUL   3  NH4    16(H4 N 1+)                                                  
FORMUL   8   CL    4(CL 1-)                                                     
FORMUL   9  ZYC    2(C12 H14 O4)                                                
FORMUL  25  HOH   *907(H2 O)                                                    
HELIX    1   1 THR A   40  GLU A   53  1                                  14    
HELIX    2   2 LYS A   71  MET A   75  5                                   5    
HELIX    3   3 THR A   76  THR A   93  1                                  18    
HELIX    4   4 ALA A  106  TYR A  119  1                                  14    
HELIX    5   5 ALA A  133  GLY A  142  1                                  10    
HELIX    6   6 GLY A  167  LEU A  176  1                                  10    
HELIX    7   7 PRO A  177  ALA A  183  1                                   7    
HELIX    8   8 PRO A  202  TYR A  212  1                                  11    
HELIX    9   9 SER A  230  GLN A  244  1                                  15    
HELIX   10  10 THR B   40  GLU B   53  1                                  14    
HELIX   11  11 LYS B   71  MET B   75  5                                   5    
HELIX   12  12 THR B   76  THR B   93  1                                  18    
HELIX   13  13 GLN B  107  TYR B  119  1                                  13    
HELIX   14  14 ALA B  133  GLY B  142  1                                  10    
HELIX   15  15 GLY B  167  LEU B  176  1                                  10    
HELIX   16  16 PRO B  177  ALA B  183  1                                   7    
HELIX   17  17 PRO B  202  TYR B  212  1                                  11    
HELIX   18  18 ASP B  229  GLN B  244  1                                  16    
SHEET    1   A 8 GLY A   0  ARG A   8  0                                        
SHEET    2   A 8 LEU A  11  GLU A  19 -1  O  GLY A  15   N  ILE A   4           
SHEET    3   A 8 ALA A  56  PHE A  60 -1  O  SER A  57   N  GLU A  18           
SHEET    4   A 8 TYR A  25  PHE A  31  1  N  ILE A  30   O  VAL A  58           
SHEET    5   A 8 VAL A  97  HIS A 105  1  O  VAL A 103   N  PHE A  31           
SHEET    6   A 8 ILE A 123  LEU A 129  1  O  VAL A 127   N  LEU A 102           
SHEET    7   A 8 VAL A 189  GLY A 194  1  O  CYS A 190   N  LEU A 128           
SHEET    8   A 8 SER A 215  ILE A 220  1  O  HIS A 218   N  LEU A 191           
SHEET    1   B 2 ASN A 143  THR A 144  0                                        
SHEET    2   B 2 VAL A 147  THR A 148 -1  O  VAL A 147   N  THR A 144           
SHEET    1   C 2 ARG A 157  PHE A 160  0                                        
SHEET    2   C 2 LEU A 163  GLY A 166 -1  O  LEU A 165   N  LEU A 158           
SHEET    1   D 8 GLY B   0  ARG B   8  0                                        
SHEET    2   D 8 LEU B  11  GLU B  19 -1  O  ARG B  17   N  ALA B   2           
SHEET    3   D 8 ALA B  56  PHE B  60 -1  O  SER B  57   N  GLU B  18           
SHEET    4   D 8 TYR B  25  PHE B  31  1  N  ALA B  28   O  ALA B  56           
SHEET    5   D 8 VAL B  97  HIS B 105  1  O  VAL B 103   N  PHE B  31           
SHEET    6   D 8 ILE B 123  LEU B 129  1  O  LEU B 129   N  GLY B 104           
SHEET    7   D 8 VAL B 189  GLY B 194  1  O  CYS B 190   N  VAL B 126           
SHEET    8   D 8 SER B 215  ILE B 220  1  O  THR B 216   N  LEU B 191           
SHEET    1   E 2 ASN B 143  THR B 144  0                                        
SHEET    2   E 2 VAL B 147  THR B 148 -1  O  VAL B 147   N  THR B 144           
SHEET    1   F 2 ARG B 157  PHE B 160  0                                        
SHEET    2   F 2 LEU B 163  GLY B 166 -1  O  LEU B 165   N  LEU B 158           
SITE     1 AC1  4 ILE A  30  PHE A  31  HIS A  32  PHE A  60                    
SITE     1 AC2  6 SER A 113  ALA A 116  GLY A 117  SER A 182                    
SITE     2 AC2  6 PHE A 185  TYR A 212                                          
SITE     1 AC3  5 PHE B  72  GLU B  73  MET B  75  LEU B 165                    
SITE     2 AC3  5 GLY B 166                                                     
SITE     1 AC4  4 GLN B 175  HOH B 289  HOH B 331  HOH B 788                    
SITE     1 AC5  5 ASP A 209  TYR A 212  SER A 215  HOH A 270                    
SITE     2 AC5  5 HOH A 318                                                     
SITE     1 AC6  4 ASN A  -5  LEU A  -4  GLU A  23  HIS A  96                    
SITE     1 AC7  5 HOH A2061  LEU B  -4  ASN B  -5  GLU B  23                    
SITE     2 AC7  5 HIS B  96                                                     
SITE     1 AC8  5 LYS B  71  PHE B  72  GLU B  73  ASP B 162                    
SITE     2 AC8  5 HOH B 323                                                     
SITE     1 AC9  7 HIS B  32  GLY B  33  PHE B  62  GLU B  80                    
SITE     2 AC9  7 GLN B 107  GLY B 108  HOH B1524                               
SITE     1 BC1  5 THR B  40  LEU B  42  LEU B  43  HOH B 627                    
SITE     2 BC1  5 HOH B1527                                                     
SITE     1 BC2  3 HOH B 782  HOH B1061  HOH B1646                               
SITE     1 BC3  5 GLY B 166  GLY B 167  PHE B 168  HOH B 556                    
SITE     2 BC3  5 HOH B 747                                                     
SITE     1 BC4  2 ASN A 150  ASP A 152                                          
SITE     1 BC5  5 THR B  40  SER B  41   CL B 261  HOH B 628                    
SITE     2 BC5  5 HOH B2117                                                     
SITE     1 BC6  1 HOH B2034                                                     
SITE     1 BC7  1 THR B  35                                                     
SITE     1 BC8  3 SER B  41  ARG B  44  NH4 B 258                               
SITE     1 BC9  4 ASN B 234  ASN B 237  HOH B 330  HOH B 841                    
SITE     1 CC1  6 ASP A 156  GLY A 166  GLY A 167  PHE A 168                    
SITE     2 CC1  6 HOH A 909  HOH B 349                                          
SITE     1 CC2  3 LEU B  -4  PHE B  21  GLY B  22                               
SITE     1 CC3 12 GLY B  33  PHE B  34  ALA B 106  GLN B 107                    
SITE     2 CC3 12 LEU B 135  ASP B 138  GLN B 145  TYR B 169                    
SITE     3 CC3 12 HIS B 225  HOH B1532  HOH B1538  HOH B1608                    
SITE     1 CC4 13 GLY A  33  PHE A  34  ALA A 106  GLN A 107                    
SITE     2 CC4 13 ALA A 132  LEU A 135  ASP A 138  THR A 144                    
SITE     3 CC4 13 GLN A 145  TYR A 169  HIS A 225  HOH A2006                    
SITE     4 CC4 13 HOH A2055                                                     
CRYST1   72.260   83.891   88.947  90.00  98.21  90.00 C 1 2 1       8          
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      0.013839  0.000000  0.001996        0.00000                         
SCALE2      0.000000  0.011920  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011359        0.00000                         
TER    1966      GLN A 244                                                      
TER    3941      GLN B 244                                                      
MASTER      503    0   22   18   24    0   37    6 4867    2   32   42          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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