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LongText Report for: 3QM1-pdb

Name Class
3QM1-pdb
HEADER    HYDROLASE                               03-FEB-11   3QM1              
TITLE     CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE   
TITLE    2 LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE, FORM II           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CINNAMOYL ESTERASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 22-265;                                       
COMPND   5 EC: 3.1.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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, CINNAMOYL/FERULOYL ESTERASE,               
KEYWDS   2 HYDROXYCINAMMATES, HYDROLASE                                         
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 3QM1    0                                                
JRNL        AUTH   K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,A.MOLLOY,A.SAVCHENKO,    
JRNL        AUTH 2 A.YAKUNIN,C.F.GONZALEZ                                       
JRNL        TITL   AN INSERTED α/β SUBDOMAIN SHAPES THE CATALYTIC     
JRNL        TITL 2 POCKET OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE         
JRNL        REF    PLOS ONE                                   2011              
JRNL        REFN                   ESSN 1932-6203                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22353                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1119                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 23.0686 -  3.6294    1.00     2836   150  0.1391 0.1664        
REMARK   3     2  3.6294 -  2.8825    1.00     2740   145  0.1405 0.1783        
REMARK   3     3  2.8825 -  2.5186    0.99     2688   140  0.1529 0.2021        
REMARK   3     4  2.5186 -  2.2886    0.98     2666   138  0.1422 0.2115        
REMARK   3     5  2.2886 -  2.1247    0.98     2631   141  0.1385 0.1890        
REMARK   3     6  2.1247 -  1.9995    0.98     2608   137  0.1392 0.2088        
REMARK   3     7  1.9995 -  1.8994    0.95     2560   135  0.1636 0.1941        
REMARK   3     8  1.8994 -  1.8168    0.94     2505   133  0.2268 0.2669        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 42.33                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.720           
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) : 3.40240                                              
REMARK   3    B22 (A**2) : -2.42420                                             
REMARK   3    B33 (A**2) : -0.97820                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.016           2056                                  
REMARK   3   ANGLE     :  1.710           2809                                  
REMARK   3   CHIRALITY :  0.116            320                                  
REMARK   3   PLANARITY :  0.010            371                                  
REMARK   3   DIHEDRAL  : 13.380            760                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resid -5:179                               
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4870  11.4229  -7.4499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0828 T22:   0.0923                                     
REMARK   3      T33:   0.1351 T12:   0.0051                                     
REMARK   3      T13:   0.0380 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4086 L22:   1.7207                                     
REMARK   3      L33:   0.2404 L12:   0.2283                                     
REMARK   3      L13:   0.0093 L23:  -0.6127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0232 S12:   0.0146 S13:   0.0181                       
REMARK   3      S21:  -0.2004 S22:  -0.0690 S23:  -0.3415                       
REMARK   3      S31:   0.0450 S32:   0.0197 S33:   0.0879                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resid 180:244                              
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5993  18.5354 -13.7587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1073 T22:   0.1082                                     
REMARK   3      T33:   0.0946 T12:  -0.0029                                     
REMARK   3      T13:  -0.0131 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2407 L22:   1.8123                                     
REMARK   3      L33:   0.9886 L12:  -0.2012                                     
REMARK   3      L13:   0.2229 L23:  -0.9612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:   0.0422 S13:   0.0724                       
REMARK   3      S21:  -0.2784 S22:   0.0627 S23:   0.1516                       
REMARK   3      S31:   0.0905 S32:  -0.1782 S33:  -0.0837                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063814.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-10                          
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   : 22853                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200   FOR THE DATA SET  : 27.5600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32600                            
REMARK 200   FOR SHELL         : 3.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB CODE 3PF8                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M AMMONIUM        
REMARK 280  SULPHATE, 24% PEG3350, 25 MM ETHYL FERULATE, 1/10 V8 PROTEASE,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       40.57100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.57100            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.93600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.69800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.93600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.69800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.57100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.93600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.69800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.57100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.93600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.69800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 302  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 456  LIES ON A SPECIAL POSITION.                          
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 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     GLU A   7    CG   CD   OE1  OE2                                  
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 A  78   CB  -  CG  -  CD1 ANGL. DEV. = -11.3 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     -129.04     57.58                                   
REMARK 500    ALA A  36     -159.52    -94.44                                   
REMARK 500    ARG A  98      -80.86    -95.79                                   
REMARK 500    ALA A 106     -120.20     63.73                                   
REMARK 500    HIS A 153       73.27   -155.56                                   
REMARK 500    LYS A 161     -125.38     57.20                                   
REMARK 500    ASP A 229     -114.51     53.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 466        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 467        DISTANCE =  5.35 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE BOND ANGLE OAL-CAM-OAC, WITH A VALUE OF 116 DEGREES, IS MODELED  
REMARK 600 IN UNAMBIGUOUS ELECTRON DENSITY TO CONTAIN PARTIAL CHIRAL CHARACTER  
REMARK 600 PERHAPS DUE TO THE FACT THAT THIS LIGAND IS BOUND TO A               
REMARK 600 CATALYTICALLY INACTIVE MUTANT, S106A, OF THE LJ0536 ENZYME. BOND IS  
REMARK 600 STRAINED FROM IDEAL OF 120 DEGREES AS ENZYME COULD HAVE TRAPPED      
REMARK 600 SUBSTRATE IN A PSEUDO-TRANSITION STATE OF THE HYDROLYSIS REACTION,   
REMARK 600 PRESUMED TO CONTAIN A TETRAHEDRAL TRANSITION STATE WITH A OAL-CAM-   
REMARK 600 OAC BOND ANGLE OF 109 DEGREES                                        
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 282  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 479   O                                                      
REMARK 620 2 ASP A 209   O   158.4                                              
REMARK 620 3 TYR A 212   O    94.3 107.1                                        
REMARK 620 4 SER A 215   OG   93.4  83.5 106.6                                  
REMARK 620 5 HOH A 385   O   103.8  77.5  80.5 161.0                            
REMARK 620 6 HOH A 438   O    71.7  86.9 166.0  74.6 102.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 276  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  63   OD1                                                    
REMARK 620 2 LYS A  71   O   116.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 246  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 439   O                                                      
REMARK 620 2 HOH A 469   O   101.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 263  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 388   O                                                      
REMARK 620 2 HOH A 353   O   119.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 275  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 413   O                                                      
REMARK 620 2 HOH A 388   O    91.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 257  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 447   O                                                      
REMARK 620 2 GLN A  -1   O   110.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 250  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 423   O                                                      
REMARK 620 2 HOH A 476   O   136.1                                              
REMARK 620 3 HOH A 407   O   155.1  68.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 255  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  67   O                                                      
REMARK 620 2 ASP A  69   OD1 115.6                                              
REMARK 620 3 GLN A  12   OE1 128.5 115.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 267  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 348   O                                                      
REMARK 620 2 HOH A 467   O   137.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 253  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 362   O                                                      
REMARK 620 2 GLN A 175   O   120.1                                              
REMARK 620 3 HOH A 344   O   120.7 110.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 258  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 157   O                                                      
REMARK 620 2 HOH A 441   O   114.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 283  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 422   O                                                      
REMARK 620 2 HOH A 411   O    91.2                                              
REMARK 620 3 HOH A 352   O   103.5 115.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 280  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 196   OD2                                                    
REMARK 620 2 GLY A 222   O    72.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 271  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 149   O                                                      
REMARK 620 2 GLY A 142   O    65.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 285  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 209   OD2                                                    
REMARK 620 2 HOH A 426   O    87.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYC A 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 248                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 249                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 251                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 252                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 253                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 254                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 255                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 256                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 257                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 258                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 259                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 260                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 261                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 264                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 266                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 268                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 269                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 270                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 271                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 272                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 274                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 275                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 276                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 277                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 278                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 279                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 280                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 281                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 282                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 283                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 284                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 285                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 286                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 287                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 288                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 289                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 290                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 291                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 292                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 293                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 294                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 295                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 296                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 297                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306                  
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: 3PFB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE           
REMARK 900 RELATED ID: 3PFC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 MUTANT IN COMPLEX WITH FERULIC ACID                  
DBREF  3QM1 A    1   244  UNP    D3YEX6   D3YEX6_LACJO     1    244             
SEQADV 3QM1 MET A  -20  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 GLY A  -19  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 SER A  -18  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 SER A  -17  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -16  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -15  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -14  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -13  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -12  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 HIS A  -11  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 SER A  -10  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 SER A   -9  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 GLY A   -8  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 ARG A   -7  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 GLU A   -6  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 ASN A   -5  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 LEU A   -4  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 TYR A   -3  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 PHE A   -2  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 GLN A   -1  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 GLY A    0  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3QM1 ALA A  106  UNP  D3YEX6    SER   106 ENGINEERED MUTATION            
SEQRES   1 A  265  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  265  ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR          
SEQRES   3 A  265  LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU          
SEQRES   4 A  265  GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE          
SEQRES   5 A  265  HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG          
SEQRES   6 A  265  GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER          
SEQRES   7 A  265  VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY          
SEQRES   8 A  265  LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP          
SEQRES   9 A  265  ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS          
SEQRES  10 A  265  VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY          
SEQRES  11 A  265  VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU          
SEQRES  12 A  265  ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU          
SEQRES  13 A  265  LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR          
SEQRES  14 A  265  TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS          
SEQRES  15 A  265  ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN          
SEQRES  16 A  265  GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS          
SEQRES  17 A  265  PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL          
SEQRES  18 A  265  SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN          
SEQRES  19 A  265  ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS          
SEQRES  20 A  265  PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR          
SEQRES  21 A  265  THR ASP PHE LEU GLN                                          
HET    ZYC  A 245      16                                                       
HET     NA  A 246       1                                                       
HET     NA  A 247       1                                                       
HET     NA  A 248       1                                                       
HET     NA  A 249       1                                                       
HET     NA  A 250       1                                                       
HET     NA  A 251       1                                                       
HET     NA  A 252       1                                                       
HET     NA  A 253       1                                                       
HET     NA  A 254       1                                                       
HET     NA  A 255       1                                                       
HET     NA  A 256       1                                                       
HET     NA  A 257       1                                                       
HET     NA  A 258       1                                                       
HET     NA  A 259       1                                                       
HET     NA  A 260       1                                                       
HET     NA  A 261       1                                                       
HET     NA  A 262       1                                                       
HET     NA  A 263       1                                                       
HET     NA  A 264       1                                                       
HET     NA  A 265       1                                                       
HET     NA  A 266       1                                                       
HET     NA  A 267       1                                                       
HET     NA  A 268       1                                                       
HET     NA  A 269       1                                                       
HET     NA  A 270       1                                                       
HET     NA  A 271       1                                                       
HET     NA  A 272       1                                                       
HET     NA  A 273       1                                                       
HET     NA  A 274       1                                                       
HET     NA  A 275       1                                                       
HET     NA  A 276       1                                                       
HET     NA  A 277       1                                                       
HET     NA  A 278       1                                                       
HET     NA  A 279       1                                                       
HET     NA  A 280       1                                                       
HET     NA  A 281       1                                                       
HET     NA  A 282       1                                                       
HET     NA  A 283       1                                                       
HET     NA  A 284       1                                                       
HET     NA  A 285       1                                                       
HET     NA  A 286       1                                                       
HET     NA  A 287       1                                                       
HET     CL  A 288       1                                                       
HET     CL  A 289       1                                                       
HET     CL  A 290       1                                                       
HET     CL  A 291       1                                                       
HET     CL  A 292       1                                                       
HET     CL  A 293       1                                                       
HET     CL  A 294       1                                                       
HET     CL  A 295       1                                                       
HET     CL  A 296       1                                                       
HET     CL  A 297       1                                                       
HET     CL  A 298       1                                                       
HET     CL  A 299       1                                                       
HET     CL  A 300       1                                                       
HET     CL  A 301       1                                                       
HET     CL  A 302       1                                                       
HET     CL  A 303       1                                                       
HET     CL  A 304       1                                                       
HET     CL  A 305       1                                                       
HET     CL  A 306       1                                                       
HETNAM     ZYC ETHYL (2E)-3-(4-HYDROXY-3-METHOXYPHENYL)PROP-2-ENOATE            
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     ZYC ETHYL FERULATE                                                   
FORMUL   2  ZYC    C12 H14 O4                                                   
FORMUL   3   NA    42(NA 1+)                                                    
FORMUL  45   CL    19(CL 1-)                                                    
FORMUL  64  HOH   *173(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  GLN A  175  1                                   9    
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  228  SER A  230  5                                   3    
HELIX   10  10 TYR A  231  GLN A  244  1                                  14    
SHEET    1   A 8 GLY A   0  ARG A   8  0                                        
SHEET    2   A 8 LEU A  11  GLU A  19 -1  O  GLU A  19   N  GLY A   0           
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  TYR A 101   N  ILE A  29           
SHEET    6   A 8 ILE A 123  LEU A 129  1  O  LYS A 124   N  ILE A 100           
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           
LINK        NA    NA A 282                 O   HOH A 479     1555   1555  2.39  
LINK         O   ASP A 209                NA    NA A 282     1555   1555  2.42  
LINK         O   TYR A 212                NA    NA A 282     1555   1555  2.46  
LINK         OG  SER A 215                NA    NA A 282     1555   1555  2.58  
LINK        NA    NA A 272                 O   HOH A 477     1555   1555  2.64  
LINK         OD1 ASN A  63                NA    NA A 276     1555   1555  2.67  
LINK        NA    NA A 246                 O   HOH A 439     1555   1555  2.67  
LINK        NA    NA A 263                 O   HOH A 388     1555   1555  2.71  
LINK        NA    NA A 282                 O   HOH A 385     1555   1555  2.71  
LINK        NA    NA A 275                 O   HOH A 413     1555   1555  2.72  
LINK        NA    NA A 257                 O   HOH A 447     1555   1555  2.73  
LINK        NA    NA A 275                 O   HOH A 388     1555   1555  2.73  
LINK        NA    NA A 269                 O   HOH A 475     1555   1555  2.75  
LINK        NA    NA A 250                 O   HOH A 423     1555   1555  2.76  
LINK         O   ASP A  67                NA    NA A 255     1555   1555  2.76  
LINK        NA    NA A 267                 O   HOH A 348     1555   1555  2.77  
LINK        NA    NA A 253                 O   HOH A 362     1555   1555  2.78  
LINK        NA    NA A 263                 O   HOH A 353     1555   1555  2.80  
LINK         O   GLN A 175                NA    NA A 253     1555   1555  2.81  
LINK         O   LYS A  71                NA    NA A 276     1555   1555  2.82  
LINK         OD1 ASP A  69                NA    NA A 255     1555   1555  2.84  
LINK        NA    NA A 253                 O   HOH A 344     1555   1555  2.86  
LINK         O   ARG A 157                NA    NA A 258     1555   1555  2.87  
LINK        NA    NA A 283                 O   HOH A 422     1555   1555  2.88  
LINK        NA    NA A 258                 O   HOH A 441     1555   1555  2.88  
LINK        NA    NA A 283                 O   HOH A 411     1555   1555  2.89  
LINK        NA    NA A 283                 O   HOH A 352     1555   1555  2.92  
LINK         OD2AASP A 196                NA    NA A 280     1555   1555  2.92  
LINK        NA    NA A 277                 O   HOH A 355     1555   1555  2.96  
LINK        NA    NA A 246                 O   HOH A 469     1555   1555  2.98  
LINK        NA    NA A 267                 O   HOH A 467     1555   1555  3.00  
LINK        NA    NA A 254                 O   HOH A 370     1555   1555  3.04  
LINK         O   TYR A 149                NA    NA A 271     1555   1555  3.06  
LINK         O   GLN A  -1                NA    NA A 257     1555   1555  3.06  
LINK         O   GLY A 142                NA    NA A 271     1555   1555  3.07  
LINK        NA    NA A 249                 O   HOH A 352     1555   1555  3.08  
LINK         OG1 THR A 198                NA    NA A 284     1555   1555  3.10  
LINK         OE1 GLN A  12                NA    NA A 255     1555   1555  3.10  
LINK         OE1 GLU A 180                NA    NA A 264     1555   1555  3.10  
LINK         O   PRO A 151                NA    NA A 256     1555   1555  3.11  
LINK         OD2 ASP A 209                NA    NA A 285     1555   1555  3.11  
LINK         O   GLY A 222                NA    NA A 280     1555   1555  3.11  
LINK        NA    NA A 250                 O   HOH A 476     1555   1555  3.14  
LINK         OG1BTHR A 148                NA    NA A 287     1555   1555  3.14  
LINK        NA    NA A 285                 O   HOH A 426     1555   1555  3.14  
LINK         OE1 GLN A 210                NA    NA A 259     1555   1555  3.18  
LINK        NA    NA A 250                 O   HOH A 407     1555   1555  3.18  
LINK        NA    NA A 282                 O   HOH A 438     1555   1555  3.20  
SITE     1 AC1 12 GLY A  33  PHE A  34  ALA A 106  GLN A 107                    
SITE     2 AC1 12 LEU A 135  ASP A 138  THR A 144  GLN A 145                    
SITE     3 AC1 12 TYR A 169  HIS A 225   NA A 267  HOH A 338                    
SITE     1 AC2  6 LYS A  71  PHE A  72  GLU A  73  ASP A 162                    
SITE     2 AC2  6 HOH A 439  HOH A 469                                          
SITE     1 AC3  1 GLU A  23                                                     
SITE     1 AC4  1 HOH A 352                                                     
SITE     1 AC5  2 GLN A 175  HOH A 423                                          
SITE     1 AC6  1 LEU A 217                                                     
SITE     1 AC7  4 LEU A 219  ILE A 220  GLU A 221   CL A 288                    
SITE     1 AC8  3 GLN A 175  HOH A 344  HOH A 362                               
SITE     1 AC9  1 HOH A 370                                                     
SITE     1 BC1  3 GLN A  12  ASP A  67  ASP A  69                               
SITE     1 BC2  6 PRO A 151  ASP A 152  HIS A 153  ILE A 154                    
SITE     2 BC2  6 ARG A 171  HOH A 357                                          
SITE     1 BC3  3 GLN A  -1  PHE A  -2  HOH A 447                               
SITE     1 BC4  3 ARG A 157  PRO A 159  HOH A 441                               
SITE     1 BC5  3 LYS A 206  ASP A 209  GLN A 210                               
SITE     1 BC6  2 GLU A 141  LYS A 233                                          
SITE     1 BC7  2 MET A   1  ALA A   2                                          
SITE     1 BC8  3 GLY A 137  HOH A 353  HOH A 388                               
SITE     1 BC9  5 LYS A 136  ILE A 178  TYR A 179  GLU A 180                    
SITE     2 BC9  5  CL A 303                                                     
SITE     1 CC1  1 GLY A  70                                                     
SITE     1 CC2  4 ALA A  36  ZYC A 245  HOH A 348  HOH A 467                    
SITE     1 CC3  1  CL A 302                                                     
SITE     1 CC4  2  CL A 305  HOH A 475                                          
SITE     1 CC5  2 GLY A  66   CL A 301                                          
SITE     1 CC6  5 GLU A 141  GLY A 142  THR A 148  TYR A 149                    
SITE     2 CC6  5 ASN A 237                                                     
SITE     1 CC7  4 SER A 228  ASP A 229  SER A 230  HOH A 477                    
SITE     1 CC8  1 ARG A  51                                                     
SITE     1 CC9  5 LYS A 136   CL A 300   CL A 303  HOH A 388                    
SITE     2 CC9  5 HOH A 413                                                     
SITE     1 DC1  4 ASN A  63  GLY A  70  LYS A  71  HOH A 346                    
SITE     1 DC2  4 CYS A 190  HIS A 218  PHE A 242  HOH A 355                    
SITE     1 DC3  2 GLY A  10   CL A 299                                          
SITE     1 DC4  1  CL A 296                                                     
SITE     1 DC5  4 LYS A 124  ASP A 196  GLY A 222  TYR A 231                    
SITE     1 DC6  1 LEU A 217                                                     
SITE     1 DC7  5 ASP A 209  TYR A 212  SER A 215  HOH A 385                    
SITE     2 DC7  5 HOH A 479                                                     
SITE     1 DC8  3 HOH A 352  HOH A 411  HOH A 422                               
SITE     1 DC9  3 THR A 198  ASP A 224  HIS A 225                               
SITE     1 EC1  1 ASP A 209                                                     
SITE     1 EC2  1  CL A 298                                                     
SITE     1 EC3  2 GLY A 146  THR A 148                                          
SITE     1 EC4  3 HIS A 153   NA A 252  HOH A 334                               
SITE     1 EC5  2 GLU A 180   CL A 294                                          
SITE     1 EC6  3 SER A  41  ARG A  44   CL A 297                               
SITE     1 EC7  2 HOH A 377  HOH A 466                                          
SITE     1 EC8  4 SER A 113  SER A 182  PHE A 185  TYR A 212                    
SITE     1 EC9  2 THR A 195  HOH A 459                                          
SITE     1 FC1  1  CL A 289                                                     
SITE     1 FC2  3 ARG A  98  HOH A 435  HOH A 436                               
SITE     1 FC3  3 THR A   5  ASN A 214   NA A 279                               
SITE     1 FC4  2 ARG A  44   CL A 290                                          
SITE     1 FC5  4 GLU A  45  GLN A 232   NA A 286  HOH A 378                    
SITE     1 FC6  1  NA A 278                                                     
SITE     1 FC7  4 TYR A 179  LYS A 207   NA A 275  HOH A 391                    
SITE     1 FC8  5 SER A  68  GLY A  70   NA A 270  HOH A 472                    
SITE     2 FC8  5 HOH A 473                                                     
SITE     1 FC9  1  NA A 268                                                     
SITE     1 GC1  3 LYS A 136   NA A 264   NA A 275                               
SITE     1 GC2  1  NA A 269                                                     
SITE     1 GC3  3 ASN A  -5  LEU A  -4  HIS A  96                               
CRYST1   71.872   85.396   81.142  90.00  90.00  90.00 C 2 2 21      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      0.013914  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012324        0.00000                         
TER    1987      GLN A 244                                                      
MASTER      721    0   62   10   12    0   66    6 2201    1   88   21          
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.
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