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Database: PDB
Entry: 2VCY
LinkDB: 2VCY
Original site: 2VCY 
HEADER    OXIDOREDUCTASE                          28-SEP-07   2VCY              
TITLE     CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANS-2-ENOYL-COA REDUCTASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 31-373;                                           
COMPND   5 SYNONYM: HSNRBF-1, NRBF-1;                                           
COMPND   6 EC: 1.3.1.38;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET23                                     
KEYWDS    NADP, POLYMORPHISM, MITOCHONDRION, OXIDOREDUCTASE, FATTY ACID         
KEYWDS   2 BIOSYNTHESIS, ENOYL THIOESTER REDUCTASE, LIPID SYNTHESIS, TRANSIT    
KEYWDS   3 PEPTIDE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.HAAPALAINEN,R.PUDAS,O.S.SMART,R.K.WIERENGA                        
REVDAT   3   24-JUL-19 2VCY    1       REMARK                                   
REVDAT   2   24-FEB-09 2VCY    1       VERSN                                    
REVDAT   1   03-JUN-08 2VCY    0                                                
JRNL        AUTH   Z.J.CHEN,R.PUDAS,S.SHARMA,O.S.SMART,A.H.JUFFER,J.K.HILTUNEN, 
JRNL        AUTH 2 R.K.WIERENGA,A.M.HAAPALAINEN                                 
JRNL        TITL   STRUCTURAL ENZYMOLOGICAL STUDIES OF 2-ENOYL THIOESTER        
JRNL        TITL 2 REDUCTASE OF THE HUMAN MITOCHONDRIAL FAS II PATHWAY: NEW     
JRNL        TITL 3 INSIGHTS INTO ITS SUBSTRATE RECOGNITION PROPERTIES.          
JRNL        REF    J.MOL.BIOL.                   V. 379   830 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18479707                                                     
JRNL        DOI    10.1016/J.JMB.2008.04.041                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.1.1                                     
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27176                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.207                          
REMARK   3   FREE R VALUE                      : 0.267                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1391                           
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   (ANGSTROMS) : NULL                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : NULL                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 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            : 5056                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 290                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 31-41 ARE NOT PRESENT IN THE     
REMARK   3  STRUCTURE                                                           
REMARK   4                                                                      
REMARK   4 2VCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290031931.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9421                             
REMARK 200  MONOCHROMATOR                  : FIXED WITH DOUBLE CRYSTAL SI 111   
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GUF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 100 MM TRIS HCL,    
REMARK 280  PH 8.5                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.31000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.31000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       73.28000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.31000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.31000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       73.28000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.31000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.31000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       73.28000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.31000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.31000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       73.28000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     PRO A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     MET B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     TYR B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     SER B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     PRO B    40                                                      
REMARK 465     ALA B    41                                                      
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    PRO A 292   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    PRO A 292   C   -  N   -  CD  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    PRO A 343   C   -  N   -  CD  ANGL. DEV. = -20.2 DEGREES          
REMARK 500    PRO B 130   C   -  N   -  CD  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    PRO B 157   C   -  N   -  CA  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    PRO B 292   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO B 292   C   -  N   -  CD  ANGL. DEV. = -16.7 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    ASN A  93       79.91   -107.57                                   
REMARK 500    SER A 117      -37.79    -34.76                                   
REMARK 500    VAL A 166      -81.34   -116.00                                   
REMARK 500    ALA A 206       -6.80    -59.18                                   
REMARK 500    MET A 247      -33.19   -143.16                                   
REMARK 500    LYS A 252      -36.91   -134.37                                   
REMARK 500    VAL A 264      -62.10    -99.34                                   
REMARK 500    ALA A 344      116.85    -39.33                                   
REMARK 500    ALA B  55       -4.33    -53.95                                   
REMARK 500    VAL B  68       41.14    -69.06                                   
REMARK 500    ARG B  69       96.55    -52.54                                   
REMARK 500    SER B 117      -36.13    -34.28                                   
REMARK 500    VAL B 166      -86.67   -116.31                                   
REMARK 500    GLU B 246       67.58    -69.82                                   
REMARK 500    MET B 247      -32.28   -140.52                                   
REMARK 500    LYS B 252      -40.33   -140.70                                   
REMARK 500    PRO B 292      171.31    -54.03                                   
REMARK 500    LEU B 350      -28.27    -39.83                                   
REMARK 500    ILE B 365      119.12    -39.35                                   
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 A2064        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B2008        DISTANCE =  6.34 ANGSTROMS                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1378                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1378                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1379                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZSY   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF HUMAN MITOCHONDRIAL 2-ENOYL THIOESTERREDUCTASE      
REMARK 900 (CGI-63)                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT DOES NOT CONTAIN MITOCHONDRIAL SIGNAL AND             
REMARK 999 STARTS FROM RESIDUE ALA31.                                           
DBREF  2VCY A   30    30  PDB    2VCY     2VCY            30     30             
DBREF  2VCY A   31   373  UNP    Q9BV79   MECR_HUMAN      31    373             
DBREF  2VCY B   30    30  PDB    2VCY     2VCY            30     30             
DBREF  2VCY B   31   373  UNP    Q9BV79   MECR_HUMAN      31    373             
SEQRES   1 A  344  MET ALA SER SER TYR SER ALA SER ALA GLU PRO ALA ARG          
SEQRES   2 A  344  VAL ARG ALA LEU VAL TYR GLY HIS HIS GLY ASP PRO ALA          
SEQRES   3 A  344  LYS VAL VAL GLU LEU LYS ASN LEU GLU LEU ALA ALA VAL          
SEQRES   4 A  344  ARG GLY SER ASP VAL ARG VAL LYS MET LEU ALA ALA PRO          
SEQRES   5 A  344  ILE ASN PRO SER ASP ILE ASN MET ILE GLN GLY ASN TYR          
SEQRES   6 A  344  GLY LEU LEU PRO GLU LEU PRO ALA VAL GLY GLY ASN GLU          
SEQRES   7 A  344  GLY VAL ALA GLN VAL VAL ALA VAL GLY SER ASN VAL THR          
SEQRES   8 A  344  GLY LEU LYS PRO GLY ASP TRP VAL ILE PRO ALA ASN ALA          
SEQRES   9 A  344  GLY LEU GLY THR TRP ARG THR GLU ALA VAL PHE SER GLU          
SEQRES  10 A  344  GLU ALA LEU ILE GLN VAL PRO SER ASP ILE PRO LEU GLN          
SEQRES  11 A  344  SER ALA ALA THR LEU GLY VAL ASN PRO CYS THR ALA TYR          
SEQRES  12 A  344  ARG MET LEU MET ASP PHE GLU GLN LEU GLN PRO GLY ASP          
SEQRES  13 A  344  SER VAL ILE GLN ASN ALA SER ASN SER GLY VAL GLY GLN          
SEQRES  14 A  344  ALA VAL ILE GLN ILE ALA ALA ALA LEU GLY LEU ARG THR          
SEQRES  15 A  344  ILE ASN VAL VAL ARG ASP ARG PRO ASP ILE GLN LYS LEU          
SEQRES  16 A  344  SER ASP ARG LEU LYS SER LEU GLY ALA GLU HIS VAL ILE          
SEQRES  17 A  344  THR GLU GLU GLU LEU ARG ARG PRO GLU MET LYS ASN PHE          
SEQRES  18 A  344  PHE LYS ASP MET PRO GLN PRO ARG LEU ALA LEU ASN CYS          
SEQRES  19 A  344  VAL GLY GLY LYS SER SER THR GLU LEU LEU ARG GLN LEU          
SEQRES  20 A  344  ALA ARG GLY GLY THR MET VAL THR TYR GLY GLY MET ALA          
SEQRES  21 A  344  LYS GLN PRO VAL VAL ALA SER VAL SER LEU LEU ILE PHE          
SEQRES  22 A  344  LYS ASP LEU LYS LEU ARG GLY PHE TRP LEU SER GLN TRP          
SEQRES  23 A  344  LYS LYS ASP HIS SER PRO ASP GLN PHE LYS GLU LEU ILE          
SEQRES  24 A  344  LEU THR LEU CYS ASP LEU ILE ARG ARG GLY GLN LEU THR          
SEQRES  25 A  344  ALA PRO ALA CYS SER GLN VAL PRO LEU GLN ASP TYR GLN          
SEQRES  26 A  344  SER ALA LEU GLU ALA SER MET LYS PRO PHE ILE SER SER          
SEQRES  27 A  344  LYS GLN ILE LEU THR MET                                      
SEQRES   1 B  344  MET ALA SER SER TYR SER ALA SER ALA GLU PRO ALA ARG          
SEQRES   2 B  344  VAL ARG ALA LEU VAL TYR GLY HIS HIS GLY ASP PRO ALA          
SEQRES   3 B  344  LYS VAL VAL GLU LEU LYS ASN LEU GLU LEU ALA ALA VAL          
SEQRES   4 B  344  ARG GLY SER ASP VAL ARG VAL LYS MET LEU ALA ALA PRO          
SEQRES   5 B  344  ILE ASN PRO SER ASP ILE ASN MET ILE GLN GLY ASN TYR          
SEQRES   6 B  344  GLY LEU LEU PRO GLU LEU PRO ALA VAL GLY GLY ASN GLU          
SEQRES   7 B  344  GLY VAL ALA GLN VAL VAL ALA VAL GLY SER ASN VAL THR          
SEQRES   8 B  344  GLY LEU LYS PRO GLY ASP TRP VAL ILE PRO ALA ASN ALA          
SEQRES   9 B  344  GLY LEU GLY THR TRP ARG THR GLU ALA VAL PHE SER GLU          
SEQRES  10 B  344  GLU ALA LEU ILE GLN VAL PRO SER ASP ILE PRO LEU GLN          
SEQRES  11 B  344  SER ALA ALA THR LEU GLY VAL ASN PRO CYS THR ALA TYR          
SEQRES  12 B  344  ARG MET LEU MET ASP PHE GLU GLN LEU GLN PRO GLY ASP          
SEQRES  13 B  344  SER VAL ILE GLN ASN ALA SER ASN SER GLY VAL GLY GLN          
SEQRES  14 B  344  ALA VAL ILE GLN ILE ALA ALA ALA LEU GLY LEU ARG THR          
SEQRES  15 B  344  ILE ASN VAL VAL ARG ASP ARG PRO ASP ILE GLN LYS LEU          
SEQRES  16 B  344  SER ASP ARG LEU LYS SER LEU GLY ALA GLU HIS VAL ILE          
SEQRES  17 B  344  THR GLU GLU GLU LEU ARG ARG PRO GLU MET LYS ASN PHE          
SEQRES  18 B  344  PHE LYS ASP MET PRO GLN PRO ARG LEU ALA LEU ASN CYS          
SEQRES  19 B  344  VAL GLY GLY LYS SER SER THR GLU LEU LEU ARG GLN LEU          
SEQRES  20 B  344  ALA ARG GLY GLY THR MET VAL THR TYR GLY GLY MET ALA          
SEQRES  21 B  344  LYS GLN PRO VAL VAL ALA SER VAL SER LEU LEU ILE PHE          
SEQRES  22 B  344  LYS ASP LEU LYS LEU ARG GLY PHE TRP LEU SER GLN TRP          
SEQRES  23 B  344  LYS LYS ASP HIS SER PRO ASP GLN PHE LYS GLU LEU ILE          
SEQRES  24 B  344  LEU THR LEU CYS ASP LEU ILE ARG ARG GLY GLN LEU THR          
SEQRES  25 B  344  ALA PRO ALA CYS SER GLN VAL PRO LEU GLN ASP TYR GLN          
SEQRES  26 B  344  SER ALA LEU GLU ALA SER MET LYS PRO PHE ILE SER SER          
SEQRES  27 B  344  LYS GLN ILE LEU THR MET                                      
HET    SO4  A1374       5                                                       
HET    SO4  A1375       5                                                       
HET    SO4  A1376       5                                                       
HET    SO4  A1377       5                                                       
HET    SO4  A1378       5                                                       
HET    SO4  B1374       5                                                       
HET    SO4  B1375       5                                                       
HET    SO4  B1376       5                                                       
HET    SO4  B1377       5                                                       
HET    SO4  B1378       5                                                       
HET    SO4  B1379       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    11(O4 S 2-)                                                  
FORMUL  14  HOH   *290(H2 O)                                                    
HELIX    1   1 ASP A   53  VAL A   58  1                                   6    
HELIX    2   2 ASN A   83  GLY A   92  1                                  10    
HELIX    3   3 PRO A  157  GLY A  165  1                                   9    
HELIX    4   4 VAL A  166  ASP A  177  1                                  12    
HELIX    5   5 SER A  194  ALA A  206  1                                  13    
HELIX    6   6 ASP A  220  SER A  230  1                                  11    
HELIX    7   7 GLU A  239  ARG A  243  1                                   5    
HELIX    8   8 GLY A  265  LEU A  276  1                                  12    
HELIX    9   9 SER A  296  LYS A  303  1                                   8    
HELIX   10  10 TRP A  311  HIS A  319  1                                   9    
HELIX   11  11 SER A  320  ARG A  337  1                                  18    
HELIX   12  12 ASP A  352  LYS A  362  1                                  11    
HELIX   13  13 ASP B   53  VAL B   57  1                                   5    
HELIX   14  14 ASN B   83  GLY B   92  1                                  10    
HELIX   15  15 PRO B  157  ALA B  162  1                                   6    
HELIX   16  16 VAL B  166  PHE B  178  1                                  13    
HELIX   17  17 SER B  194  LEU B  207  1                                  14    
HELIX   18  18 ASP B  220  LEU B  231  1                                  12    
HELIX   19  19 GLU B  239  ARG B  243  1                                   5    
HELIX   20  20 GLY B  265  LEU B  276  1                                  12    
HELIX   21  21 SER B  296  LYS B  303  1                                   8    
HELIX   22  22 TRP B  311  ASP B  318  1                                   8    
HELIX   23  23 SER B  320  ARG B  337  1                                  18    
HELIX   24  24 ASP B  352  MET B  361  1                                  10    
SHEET    1  AA 3 GLU A  59  LEU A  63  0                                        
SHEET    2  AA 3 VAL A  43  TYR A  48 -1  O  VAL A  43   N  LEU A  63           
SHEET    3  AA 3 ALA A 102  VAL A 103 -1  O  ALA A 102   N  TYR A  48           
SHEET    1  AB 5 GLU A 141  SER A 145  0                                        
SHEET    2  AB 5 ASP A  72  PRO A  81 -1  O  VAL A  73   N  PHE A 144           
SHEET    3  AB 5 VAL A 109  VAL A 115 -1  O  VAL A 109   N  LEU A  78           
SHEET    4  AB 5 TRP A 127  PRO A 130 -1  O  VAL A 128   N  ALA A 110           
SHEET    5  AB 5 LEU A 149  VAL A 152 -1  O  ILE A 150   N  ILE A 129           
SHEET    1  AC 4 GLU A 141  SER A 145  0                                        
SHEET    2  AC 4 ASP A  72  PRO A  81 -1  O  VAL A  73   N  PHE A 144           
SHEET    3  AC 4 LYS A 368  THR A 372 -1  O  LEU A 371   N  ALA A  80           
SHEET    4  AC 4 CYS A 345  PRO A 349  1  O  SER A 346   N  ILE A 370           
SHEET    1  AD 6 HIS A 235  THR A 238  0                                        
SHEET    2  AD 6 ARG A 210  VAL A 215  1  O  THR A 211   N  HIS A 235           
SHEET    3  AD 6 SER A 186  GLN A 189  1  O  VAL A 187   N  ILE A 212           
SHEET    4  AD 6 LEU A 259  ASN A 262  1  O  LEU A 259   N  ILE A 188           
SHEET    5  AD 6 THR A 281  THR A 284  1  O  THR A 281   N  ALA A 260           
SHEET    6  AD 6 LYS A 306  GLY A 309  1  O  LYS A 306   N  MET A 282           
SHEET    1  AE 2 VAL A 293  ALA A 295  0                                        
SHEET    2  AE 2 VAL B 293  ALA B 295 -1  O  VAL B 293   N  ALA A 295           
SHEET    1  BA 3 VAL B  58  LEU B  63  0                                        
SHEET    2  BA 3 VAL B  43  TYR B  48 -1  O  VAL B  43   N  LEU B  63           
SHEET    3  BA 3 ALA B 102  VAL B 103 -1  O  ALA B 102   N  TYR B  48           
SHEET    1  BB 5 GLU B 141  SER B 145  0                                        
SHEET    2  BB 5 ASP B  72  PRO B  81 -1  O  VAL B  73   N  PHE B 144           
SHEET    3  BB 5 VAL B 109  VAL B 115 -1  O  VAL B 109   N  LEU B  78           
SHEET    4  BB 5 TRP B 127  PRO B 130 -1  O  VAL B 128   N  ALA B 110           
SHEET    5  BB 5 LEU B 149  GLN B 151 -1  O  ILE B 150   N  ILE B 129           
SHEET    1  BC 4 GLU B 141  SER B 145  0                                        
SHEET    2  BC 4 ASP B  72  PRO B  81 -1  O  VAL B  73   N  PHE B 144           
SHEET    3  BC 4 LYS B 368  THR B 372 -1  O  LEU B 371   N  ALA B  80           
SHEET    4  BC 4 CYS B 345  PRO B 349  1  O  SER B 346   N  ILE B 370           
SHEET    1  BD 6 HIS B 235  THR B 238  0                                        
SHEET    2  BD 6 ARG B 210  VAL B 215  1  O  THR B 211   N  HIS B 235           
SHEET    3  BD 6 SER B 186  ASN B 190  1  O  VAL B 187   N  ILE B 212           
SHEET    4  BD 6 LEU B 259  ASN B 262  1  O  LEU B 259   N  ILE B 188           
SHEET    5  BD 6 THR B 281  THR B 284  1  O  THR B 281   N  ALA B 260           
SHEET    6  BD 6 LYS B 306  GLY B 309  1  O  LYS B 306   N  MET B 282           
CISPEP   1 LEU A  100    PRO A  101          0        -0.23                     
CISPEP   2 LEU B  100    PRO B  101          0        -1.31                     
SITE     1 AC1  4 GLN A 256  HOH A2147  HOH A2148  HOH A2149                    
SITE     1 AC2  3 ARG A 308  HOH A2069  HOH B2100                               
SITE     1 AC3  4 ARG A 139  HOH A2047  HOH A2150  HOH A2151                    
SITE     1 AC4  4 ASN A 167  SER A 194  GLY A 195  LYS A 368                    
SITE     1 AC5  6 ALA A 191  SER A 192  ASN A 193  VAL A 215                    
SITE     2 AC5  6 ARG A 216  ARG A 218                                          
SITE     1 AC6  5 ARG A  69  PRO B 255  GLN B 256  HOH B2087                    
SITE     2 AC6  5 HOH B2133                                                     
SITE     1 AC7  5 LYS A 306  ARG B 308  HOH B2061  HOH B2134                    
SITE     2 AC7  5 HOH B2136                                                     
SITE     1 AC8  3 VAL B 103  ARG B 139  HOH B2043                               
SITE     1 AC9  3 ALA A 289  ARG B 274  SER B 296                               
SITE     1 BC1  6 PRO B  84  ASN B 167  SER B 194  GLY B 195                    
SITE     2 BC1  6 VAL B 196  LYS B 368                                          
SITE     1 BC2  7 ALA B 191  SER B 192  ASN B 193  SER B 194                    
SITE     2 BC2  7 VAL B 215  ARG B 216  ARG B 218                               
CRYST1  104.620  104.620  146.560  90.00  90.00  90.00 P 42 21 2    16          
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      0.009558  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006823        0.00000                         
MTRIX1   1 -0.147500  0.980190  0.132210      -53.60578    1                    
MTRIX2   1  0.986730  0.136660  0.087720       47.96128    1                    
MTRIX3   1  0.067910  0.143400 -0.987330      -12.56546    1                    
MTRIX1   2 -0.147500  0.986730  0.067910      -54.37840    1                    
MTRIX2   2  0.980190  0.136660  0.143400       47.79124    1                    
MTRIX3   2  0.132210  0.087720 -0.987330       -9.52591    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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