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Database: PDB
Entry: 2R2G
LinkDB: 2R2G
Original site: 2R2G 
HEADER    PLANT PROTEIN                           24-AUG-07   2R2G              
TITLE     STRUCTURE OF EUGENOL SYNTHASE FROM OCIMUM BASILICUM COMPLEXED WITH    
TITLE    2 EMDF                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUGENOL SYNTHASE 1;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OCIMUM BASILICUM;                               
SOURCE   3 ORGANISM_COMMON: SWEET BASIL;                                        
SOURCE   4 ORGANISM_TAXID: 39350;                                               
SOURCE   5 GENE: EGS1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS8                                     
KEYWDS    EUGENOL, PHENYLPROPENE, PIP REDUCTASE, SHORT-CHAIN                    
KEYWDS   2 DEHYDROGENASE/REDUCTASE, PLANT PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.V.LOUIE,J.P.NOEL,M.E.BOWMAN                                         
REVDAT   3   25-OCT-17 2R2G    1       REMARK                                   
REVDAT   2   24-FEB-09 2R2G    1       VERSN                                    
REVDAT   1   15-JAN-08 2R2G    0                                                
JRNL        AUTH   G.V.LOUIE,T.J.BAIGA,M.E.BOWMAN,T.KOEDUKA,J.H.TAYLOR,         
JRNL        AUTH 2 S.M.SPASSOVA,E.PICHERSKY,J.P.NOEL                            
JRNL        TITL   STRUCTURE AND REACTION MECHANISM OF BASIL EUGENOL SYNTHASE   
JRNL        REF    PLOS ONE                      V.   2  E993 2007              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   17912370                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0000993                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 57422                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2918                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4954                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 130                                     
REMARK   3   SOLVENT ATOMS            : 350                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.98400                                             
REMARK   3    B22 (A**2) : 0.39900                                              
REMARK   3    B33 (A**2) : 2.58500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 5.85300                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.280                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.843 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.575 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.829 ; 2.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.105 ; 4.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 47.15                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NDP.PAR                                        
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : EMF.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2R2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044340.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57391                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.151                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1QYC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM SUCCINATE, 21% PEG 3350,    
REMARK 280  0.3 M KCL, 2 MM DITHIOTHREITOL, 5 MM NADP+, PH 5.5, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.09850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS A MONOMER (HALF OF THE ASYMMETRIC UNIT)   
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
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     SER A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     ASN B     4                                                      
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    LYS A  44       34.42    -83.51                                   
REMARK 500    ASP A 111      -85.67   -113.80                                   
REMARK 500    ASN A 152     -147.60     62.92                                   
REMARK 500    ASP A 305       73.69   -161.58                                   
REMARK 500    LYS B  44       38.92    -80.81                                   
REMARK 500    ASP B 111      -83.21   -112.79                                   
REMARK 500    ASN B 152     -149.34     62.41                                   
REMARK 500    ASP B 305       75.16   -157.68                                   
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 NAP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMF A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMF B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QW8   RELATED DB: PDB                                   
REMARK 900 EUGENOL SYNTHASE, NADP+ MONOCLINIC FORM                              
REMARK 900 RELATED ID: 2QX7   RELATED DB: PDB                                   
REMARK 900 EUGENOL SYNTHASE, NADP+ ORTHORHOMBIC FORM                            
REMARK 900 RELATED ID: 2QYS   RELATED DB: PDB                                   
REMARK 900 EUGENOL SYNTHASE APO FORM                                            
REMARK 900 RELATED ID: 2QZ2   RELATED DB: PDB                                   
REMARK 900 EUGENOL SYNTHASE, NADP+, EMDF TERNARY COMPLEX                        
REMARK 900 RELATED ID: 2QZZ   RELATED DB: PDB                                   
DBREF  2R2G A    1   314  UNP    Q15GI4   Q15GI4_OCIBA     1    314             
DBREF  2R2G B    1   314  UNP    Q15GI4   Q15GI4_OCIBA     1    314             
SEQADV 2R2G SER A   -3  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLY A   -2  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G HIS A   -1  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLY A    0  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLN A  132  UNP  Q15GI4    LYS   132 ENGINEERED                     
SEQADV 2R2G SER B   -3  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLY B   -2  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G HIS B   -1  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLY B    0  UNP  Q15GI4              EXPRESSION TAG                 
SEQADV 2R2G GLN B  132  UNP  Q15GI4    LYS   132 ENGINEERED                     
SEQRES   1 A  318  SER GLY HIS GLY MET GLU GLU ASN GLY MET LYS SER LYS          
SEQRES   2 A  318  ILE LEU ILE PHE GLY GLY THR GLY TYR ILE GLY ASN HIS          
SEQRES   3 A  318  MET VAL LYS GLY SER LEU LYS LEU GLY HIS PRO THR TYR          
SEQRES   4 A  318  VAL PHE THR ARG PRO ASN SER SER LYS THR THR LEU LEU          
SEQRES   5 A  318  ASP GLU PHE GLN SER LEU GLY ALA ILE ILE VAL LYS GLY          
SEQRES   6 A  318  GLU LEU ASP GLU HIS GLU LYS LEU VAL GLU LEU MET LYS          
SEQRES   7 A  318  LYS VAL ASP VAL VAL ILE SER ALA LEU ALA PHE PRO GLN          
SEQRES   8 A  318  ILE LEU ASP GLN PHE LYS ILE LEU GLU ALA ILE LYS VAL          
SEQRES   9 A  318  ALA GLY ASN ILE LYS ARG PHE LEU PRO SER ASP PHE GLY          
SEQRES  10 A  318  VAL GLU GLU ASP ARG ILE ASN ALA LEU PRO PRO PHE GLU          
SEQRES  11 A  318  ALA LEU ILE GLU ARG GLN ARG MET ILE ARG ARG ALA ILE          
SEQRES  12 A  318  GLU GLU ALA ASN ILE PRO TYR THR TYR VAL SER ALA ASN          
SEQRES  13 A  318  CYS PHE ALA SER TYR PHE ILE ASN TYR LEU LEU ARG PRO          
SEQRES  14 A  318  TYR ASP PRO LYS ASP GLU ILE THR VAL TYR GLY THR GLY          
SEQRES  15 A  318  GLU ALA LYS PHE ALA MET ASN TYR GLU GLN ASP ILE GLY          
SEQRES  16 A  318  LEU TYR THR ILE LYS VAL ALA THR ASP PRO ARG ALA LEU          
SEQRES  17 A  318  ASN ARG VAL VAL ILE TYR ARG PRO SER THR ASN ILE ILE          
SEQRES  18 A  318  THR GLN LEU GLU LEU ILE SER ARG TRP GLU LYS LYS ILE          
SEQRES  19 A  318  GLY LYS LYS PHE LYS LYS ILE HIS VAL PRO GLU GLU GLU          
SEQRES  20 A  318  ILE VAL ALA LEU THR LYS GLU LEU PRO GLU PRO GLU ASN          
SEQRES  21 A  318  ILE PRO ILE ALA ILE LEU HIS CYS LEU PHE ILE ASP GLY          
SEQRES  22 A  318  ALA THR MET SER TYR ASP PHE LYS GLU ASN ASP VAL GLU          
SEQRES  23 A  318  ALA SER THR LEU TYR PRO GLU LEU LYS PHE THR THR ILE          
SEQRES  24 A  318  ASP GLU LEU LEU ASP ILE PHE VAL HIS ASP PRO PRO PRO          
SEQRES  25 A  318  PRO ALA SER ALA ALA PHE                                      
SEQRES   1 B  318  SER GLY HIS GLY MET GLU GLU ASN GLY MET LYS SER LYS          
SEQRES   2 B  318  ILE LEU ILE PHE GLY GLY THR GLY TYR ILE GLY ASN HIS          
SEQRES   3 B  318  MET VAL LYS GLY SER LEU LYS LEU GLY HIS PRO THR TYR          
SEQRES   4 B  318  VAL PHE THR ARG PRO ASN SER SER LYS THR THR LEU LEU          
SEQRES   5 B  318  ASP GLU PHE GLN SER LEU GLY ALA ILE ILE VAL LYS GLY          
SEQRES   6 B  318  GLU LEU ASP GLU HIS GLU LYS LEU VAL GLU LEU MET LYS          
SEQRES   7 B  318  LYS VAL ASP VAL VAL ILE SER ALA LEU ALA PHE PRO GLN          
SEQRES   8 B  318  ILE LEU ASP GLN PHE LYS ILE LEU GLU ALA ILE LYS VAL          
SEQRES   9 B  318  ALA GLY ASN ILE LYS ARG PHE LEU PRO SER ASP PHE GLY          
SEQRES  10 B  318  VAL GLU GLU ASP ARG ILE ASN ALA LEU PRO PRO PHE GLU          
SEQRES  11 B  318  ALA LEU ILE GLU ARG GLN ARG MET ILE ARG ARG ALA ILE          
SEQRES  12 B  318  GLU GLU ALA ASN ILE PRO TYR THR TYR VAL SER ALA ASN          
SEQRES  13 B  318  CYS PHE ALA SER TYR PHE ILE ASN TYR LEU LEU ARG PRO          
SEQRES  14 B  318  TYR ASP PRO LYS ASP GLU ILE THR VAL TYR GLY THR GLY          
SEQRES  15 B  318  GLU ALA LYS PHE ALA MET ASN TYR GLU GLN ASP ILE GLY          
SEQRES  16 B  318  LEU TYR THR ILE LYS VAL ALA THR ASP PRO ARG ALA LEU          
SEQRES  17 B  318  ASN ARG VAL VAL ILE TYR ARG PRO SER THR ASN ILE ILE          
SEQRES  18 B  318  THR GLN LEU GLU LEU ILE SER ARG TRP GLU LYS LYS ILE          
SEQRES  19 B  318  GLY LYS LYS PHE LYS LYS ILE HIS VAL PRO GLU GLU GLU          
SEQRES  20 B  318  ILE VAL ALA LEU THR LYS GLU LEU PRO GLU PRO GLU ASN          
SEQRES  21 B  318  ILE PRO ILE ALA ILE LEU HIS CYS LEU PHE ILE ASP GLY          
SEQRES  22 B  318  ALA THR MET SER TYR ASP PHE LYS GLU ASN ASP VAL GLU          
SEQRES  23 B  318  ALA SER THR LEU TYR PRO GLU LEU LYS PHE THR THR ILE          
SEQRES  24 B  318  ASP GLU LEU LEU ASP ILE PHE VAL HIS ASP PRO PRO PRO          
SEQRES  25 B  318  PRO ALA SER ALA ALA PHE                                      
HET    NAP  A 401      48                                                       
HET    EMF  A 601      17                                                       
HET    NAP  B 401      48                                                       
HET    EMF  B 602      17                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     EMF ETHYL (1S,2S)-2-(4-HYDROXY-3-METHOXYPHENYL)                      
HETNAM   2 EMF  CYCLOPROPANECARBOXYLATE                                         
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  EMF    2(C13 H16 O4)                                                
FORMUL   7  HOH   *350(H2 O)                                                    
HELIX    1   1 ILE A   19  LEU A   30  1                                  12    
HELIX    2   2 LYS A   44  LEU A   54  1                                  11    
HELIX    3   3 GLU A   65  LYS A   74  1                                  10    
HELIX    4   4 ALA A   84  LEU A   89  5                                   6    
HELIX    5   5 ASP A   90  GLY A  102  1                                  13    
HELIX    6   6 LEU A  122  ALA A  142  1                                  21    
HELIX    7   7 ALA A  155  ARG A  164  1                                  10    
HELIX    8   8 TYR A  186  ASP A  200  1                                  15    
HELIX    9   9 PRO A  201  LEU A  204  5                                   4    
HELIX   10  10 PRO A  212  THR A  214  5                                   3    
HELIX   11  11 GLN A  219  GLY A  231  1                                  13    
HELIX   12  12 PRO A  240  LEU A  251  1                                  12    
HELIX   13  13 GLU A  255  ILE A  267  1                                  13    
HELIX   14  14 SER A  284  LEU A  286  5                                   3    
HELIX   15  15 THR A  294  ASP A  305  1                                  12    
HELIX   16  16 ILE B   19  LEU B   30  1                                  12    
HELIX   17  17 LYS B   44  LEU B   54  1                                  11    
HELIX   18  18 GLU B   65  LYS B   74  1                                  10    
HELIX   19  19 ALA B   84  LEU B   89  5                                   6    
HELIX   20  20 ASP B   90  GLY B  102  1                                  13    
HELIX   21  21 LEU B  122  ALA B  142  1                                  21    
HELIX   22  22 ALA B  155  ARG B  164  1                                  10    
HELIX   23  23 TYR B  186  ASP B  200  1                                  15    
HELIX   24  24 PRO B  201  LEU B  204  5                                   4    
HELIX   25  25 PRO B  212  THR B  214  5                                   3    
HELIX   26  26 GLN B  219  GLY B  231  1                                  13    
HELIX   27  27 PRO B  240  LEU B  251  1                                  12    
HELIX   28  28 GLU B  255  ILE B  267  1                                  13    
HELIX   29  29 SER B  284  LEU B  286  5                                   3    
HELIX   30  30 THR B  294  ASP B  305  1                                  12    
SHEET    1   A 5 ILE A  57  LYS A  60  0                                        
SHEET    2   A 5 THR A  34  THR A  38  1  N  THR A  34   O  ILE A  57           
SHEET    3   A 5 ILE A  10  PHE A  13  1  N  ILE A  10   O  TYR A  35           
SHEET    4   A 5 VAL A  78  SER A  81  1  O  VAL A  78   N  LEU A  11           
SHEET    5   A 5 ARG A 106  LEU A 108  1  O  LEU A 108   N  SER A  81           
SHEET    1   B 3 THR A 147  SER A 150  0                                        
SHEET    2   B 3 ARG A 206  ILE A 209  1  O  VAL A 208   N  TYR A 148           
SHEET    3   B 3 VAL A 281  GLU A 282  1  O  VAL A 281   N  ILE A 209           
SHEET    1   C 3 CYS A 153  PHE A 154  0                                        
SHEET    2   C 3 LYS A 181  ASN A 185  1  O  ASN A 185   N  CYS A 153           
SHEET    3   C 3 ILE A 216  THR A 218 -1  O  ILE A 217   N  PHE A 182           
SHEET    1   D 2 GLU A 171  TYR A 175  0                                        
SHEET    2   D 2 LYS A 235  VAL A 239  1  O  ILE A 237   N  ILE A 172           
SHEET    1   E 5 ILE B  57  LYS B  60  0                                        
SHEET    2   E 5 THR B  34  THR B  38  1  N  THR B  34   O  ILE B  57           
SHEET    3   E 5 ILE B  10  PHE B  13  1  N  ILE B  10   O  TYR B  35           
SHEET    4   E 5 VAL B  78  SER B  81  1  O  VAL B  78   N  LEU B  11           
SHEET    5   E 5 ARG B 106  LEU B 108  1  O  LEU B 108   N  SER B  81           
SHEET    1   F 3 THR B 147  SER B 150  0                                        
SHEET    2   F 3 ARG B 206  ILE B 209  1  O  VAL B 208   N  TYR B 148           
SHEET    3   F 3 VAL B 281  GLU B 282  1  O  VAL B 281   N  ILE B 209           
SHEET    1   G 3 CYS B 153  PHE B 154  0                                        
SHEET    2   G 3 LYS B 181  ASN B 185  1  O  ASN B 185   N  CYS B 153           
SHEET    3   G 3 ILE B 216  THR B 218 -1  O  ILE B 217   N  PHE B 182           
SHEET    1   H 2 GLU B 171  TYR B 175  0                                        
SHEET    2   H 2 LYS B 235  VAL B 239  1  O  ILE B 237   N  ILE B 172           
CISPEP   1 GLU A  253    PRO A  254          0        -0.53                     
CISPEP   2 GLU B  253    PRO B  254          0        -0.63                     
SITE     1 AC1 28 THR A  16  GLY A  17  TYR A  18  ILE A  19                    
SITE     2 AC1 28 THR A  38  ARG A  39  SER A  42  LYS A  44                    
SITE     3 AC1 28 ALA A  82  LEU A  83  PHE A  85  GLN A  87                    
SITE     4 AC1 28 SER A 110  ASP A 111  PHE A 112  ASN A 152                    
SITE     5 AC1 28 PHE A 154  PHE A 158  EMF A 601  HOH A1002                    
SITE     6 AC1 28 HOH A1015  HOH A1023  HOH A1041  HOH A1078                    
SITE     7 AC1 28 HOH A1086  HOH A1092  HOH A1126  HOH A1456                    
SITE     1 AC2 13 PHE A  85  GLY A 113  VAL A 114  ASN A 152                    
SITE     2 AC2 13 TYR A 157  PHE A 158  PRO A 258  ILE A 261                    
SITE     3 AC2 13 LEU A 262  LEU A 265  ALA A 312  PHE A 314                    
SITE     4 AC2 13 NAP A 401                                                     
SITE     1 AC3 30 THR B  16  GLY B  17  TYR B  18  ILE B  19                    
SITE     2 AC3 30 THR B  38  ARG B  39  SER B  42  LYS B  44                    
SITE     3 AC3 30 ALA B  82  LEU B  83  ALA B  84  PHE B  85                    
SITE     4 AC3 30 GLN B  87  SER B 110  ASP B 111  PHE B 112                    
SITE     5 AC3 30 ASN B 152  PHE B 154  PHE B 158  EMF B 602                    
SITE     6 AC3 30 HOH B1012  HOH B1018  HOH B1029  HOH B1032                    
SITE     7 AC3 30 HOH B1046  HOH B1061  HOH B1081  HOH B1094                    
SITE     8 AC3 30 HOH B1231  HOH B1465                                          
SITE     1 AC4 12 GLY B 113  VAL B 114  ASN B 152  TYR B 157                    
SITE     2 AC4 12 PHE B 158  PRO B 258  ILE B 261  LEU B 262                    
SITE     3 AC4 12 LEU B 265  ALA B 312  PHE B 314  NAP B 401                    
CRYST1   53.763   86.197   76.933  90.00 107.40  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018600  0.000000  0.005829        0.00000                         
SCALE2      0.000000  0.011601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013622        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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