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Database: PDB
Entry: 2J3K
LinkDB: 2J3K
Original site: 2J3K 
HEADER    OXIDOREDUCTASE                          22-AUG-06   2J3K              
TITLE     CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE       
TITLE    2 (AT5G16970)-TERNARY COMPLEX II                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NADPH-DEPENDENT OXIDOREDUCTASE 2-ALKENAL REDUCTASE;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ATAER,NADP-DEPENDENT ALKENAL DOUBLE BOND REDUCTASE P1,DBR1, 
COMPND   5 NADPH-AZODICARBONYL/QUINONE REDUCTASE,NADPH:2-ALKENAL/ONE ALPHA,BETA-
COMPND   6 HYDROGENASE,ALH,P1-ZETA-CRYSTALLIN PROTEIN,P1-ZCR;                   
COMPND   7 EC: 1.3.1.-,1.3.1.74;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   4 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   5 ORGANISM_TAXID: 3702                                                 
KEYWDS    OXIDOREDUCTASE, ARABIDOPSIS THALIANA, 4-HYDROXY-2- NONENAL, NADP,     
KEYWDS   2 TERNARY COMPLEX II, DOUBLE BOND REDUCTASE (AT5G16970)                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.YOUN,S.J.KIM,S.G.MOINUDDIN,C.LEE,D.L.BEDGAR,A.R.HARPER,L.B.DAVIN,   
AUTHOR   2 N.G.LEWIS,C.KANG                                                     
REVDAT   5   05-DEC-18 2J3K    1       COMPND SOURCE JRNL   DBREF               
REVDAT   4   24-FEB-09 2J3K    1       VERSN                                    
REVDAT   3   02-JAN-07 2J3K    1       JRNL                                     
REVDAT   2   11-OCT-06 2J3K    1       AUTHOR JRNL                              
REVDAT   1   05-OCT-06 2J3K    0                                                
JRNL        AUTH   B.YOUN,S.J.KIM,S.G.MOINUDDIN,C.LEE,D.L.BEDGAR,A.R.HARPER,    
JRNL        AUTH 2 L.B.DAVIN,N.G.LEWIS,C.KANG                                   
JRNL        TITL   MECHANISTIC AND STRUCTURAL STUDIES OF APOFORM, BINARY, AND   
JRNL        TITL 2 TERNARY COMPLEXES OF THE ARABIDOPSIS ALKENAL DOUBLE BOND     
JRNL        TITL 3 REDUCTASE AT5G16970.                                         
JRNL        REF    J. BIOL. CHEM.                V. 281 40076 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17028190                                                     
JRNL        DOI    10.1074/JBC.M605900200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 20187                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 5304                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 118                                     
REMARK   3   SOLVENT ATOMS            : 134                                     
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   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) : 0.025                           
REMARK   3   BOND ANGLES            (DEGREES) : 4.600                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2J3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 277.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07812                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23815                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY                : 5.380                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.54000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.92000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.22500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.92000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.54000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.22500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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     PRO A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     ALA A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     ALA A    69                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR B  1208     O3X  NAP B  2346              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  91   NE2   HIS A  91   CD2    -0.081                       
REMARK 500    HIS A 119   NE2   HIS A 119   CD2    -0.076                       
REMARK 500    HIS A 248   NE2   HIS A 248   CD2    -0.068                       
REMARK 500    HIS A 269   NE2   HIS A 269   CD2    -0.068                       
REMARK 500    HIS A 303   NE2   HIS A 303   CD2    -0.075                       
REMARK 500    HIS A 331   NE2   HIS A 331   CD2    -0.069                       
REMARK 500    HIS B1091   NE2   HIS B1091   CD2    -0.077                       
REMARK 500    HIS B1119   NE2   HIS B1119   CD2    -0.088                       
REMARK 500    HIS B1248   NE2   HIS B1248   CD2    -0.075                       
REMARK 500    HIS B1269   NE2   HIS B1269   CD2    -0.079                       
REMARK 500    HIS B1303   NE2   HIS B1303   CD2    -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A   6   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    VAL A   8   CG1 -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    VAL A  30   CG1 -  CB  -  CG2 ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ARG A  33   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  55   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    TYR A  72   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TYR A  72   CB  -  CG  -  CD1 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    PRO A  74   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO A  74   CA  -  N   -  CD  ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    LEU A  99   CA  -  CB  -  CG  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    LEU A 100   CA  -  CB  -  CG  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    TRP A 101   CA  -  CB  -  CG  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    TRP A 101   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP A 101   CB  -  CG  -  CD1 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    TRP A 101   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP A 101   CG  -  CD2 -  CE3 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ILE A 103   CA  -  C   -  N   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    TRP A 106   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TRP A 106   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    LEU A 129   CA  -  CB  -  CG  ANGL. DEV. =  21.1 DEGREES          
REMARK 500    TYR A 131   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR A 131   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    CYS A 151   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    TYR A 160   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TYR A 160   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ALA A 163   CA  -  C   -  N   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    VAL A 168   CG1 -  CB  -  CG2 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    MET A 179   CG  -  SD  -  CE  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    CYS A 181   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    VAL A 193   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    THR A 198   CA  -  CB  -  CG2 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    PHE A 200   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    PHE A 202   CB  -  CG  -  CD2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    PHE A 202   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU A 211   CA  -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    LYS A 219   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    GLU A 231   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    MET A 237   CA  -  CB  -  CG  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    VAL A 243   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    HIS A 248   CA  -  C   -  N   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ARG A 250   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 250   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    VAL A 253   CG1 -  CB  -  CG2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    TYR A 260   CB  -  CG  -  CD2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    TYR A 260   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASN A 264   CA  -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    VAL A 268   CG1 -  CB  -  CG2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ILE A 274   CG1 -  CB  -  CG2 ANGL. DEV. = -21.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     128 ANGLE DEVIATIONS.                             
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    GLU A  36       88.05    -53.22                                   
REMARK 500    THR A  38       55.22    -67.26                                   
REMARK 500    ASN A  39       -5.54   -145.71                                   
REMARK 500    LEU A  46      -60.56    -90.80                                   
REMARK 500    ALA A  71      147.10     78.89                                   
REMARK 500    PRO A  74      113.98    -28.52                                   
REMARK 500    ASP A  93       40.35   -109.78                                   
REMARK 500    HIS A 117       58.60   -117.00                                   
REMARK 500    ALA A 118      -50.38   -154.90                                   
REMARK 500    SER A 152       75.90     32.18                                   
REMARK 500    ALA A 167      -68.08    -11.34                                   
REMARK 500    LYS A 177       39.91    -94.17                                   
REMARK 500    MET A 178      -27.62   -140.74                                   
REMARK 500    VAL A 233      -73.74   -102.26                                   
REMARK 500    MET A 256       60.46   -150.61                                   
REMARK 500    ALA A 316       80.31      8.13                                   
REMARK 500    LYS A 321       73.51   -106.77                                   
REMARK 500    ALA A 322      -27.76   -143.39                                   
REMARK 500    LEU B1032       23.79    -76.47                                   
REMARK 500    VAL B1034       76.48    -67.95                                   
REMARK 500    THR B1038      123.59    169.88                                   
REMARK 500    PRO B1052        0.64    -69.61                                   
REMARK 500    PRO B1061      102.46    -44.38                                   
REMARK 500    ALA B1066       29.51    -68.59                                   
REMARK 500    ALA B1071      142.69     64.86                                   
REMARK 500    PRO B1074      -16.44    -34.52                                   
REMARK 500    PRO B1077      158.67    -48.80                                   
REMARK 500    ILE B1087       79.42   -119.17                                   
REMARK 500    GLU B1088      128.31     74.81                                   
REMARK 500    LYS B1096       -2.64    -31.61                                   
REMARK 500    ALA B1118      -48.51   -140.78                                   
REMARK 500    GLN B1123       36.26   -141.57                                   
REMARK 500    ASP B1126      -24.63   -163.06                                   
REMARK 500    SER B1152       62.25     23.29                                   
REMARK 500    ALA B1167      -44.36    -18.92                                   
REMARK 500    MET B1179     -169.39   -117.34                                   
REMARK 500    THR B1198      -76.19   -104.63                                   
REMARK 500    VAL B1233      -66.56    -96.11                                   
REMARK 500    ARG B1278       26.35     48.25                                   
REMARK 500    SER B1287      -39.86    -35.30                                   
REMARK 500    TYR B1290        2.42    -65.20                                   
REMARK 500    VAL B1335      -70.16    -83.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A   34     PRO A   35                 -133.33                    
REMARK 500 ALA A  322     PRO A  323                  146.74                    
REMARK 500 VAL B 1034     PRO B 1035                 -140.78                    
REMARK 500 ALA B 1322     PRO B 1323                  147.73                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 160         0.08    SIDE CHAIN                              
REMARK 500    TYR A 260         0.09    SIDE CHAIN                              
REMARK 500    TYR B1160         0.07    SIDE CHAIN                              
REMARK 500    TYR B1208         0.07    SIDE CHAIN                              
REMARK 500    TYR B1260         0.09    SIDE CHAIN                              
REMARK 500    TYR B1293         0.07    SIDE CHAIN                              
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 A2020        DISTANCE =  5.98 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNE A1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B2346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNE B2347                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2J3H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE      
REMARK 900 (AT5G16970)-APO FORM                                                 
REMARK 900 RELATED ID: 2J3I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE      
REMARK 900 (AT5G16970)-BINARY COMPLEX                                           
REMARK 900 RELATED ID: 2J3J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE      
REMARK 900 (AT5G16970)-TERNARY COMPLEX I                                        
DBREF  2J3K A    1   345  UNP    Q39172   AER_ARATH        1    345             
DBREF  2J3K B 1001  1345  UNP    Q39172   AER_ARATH        1    345             
SEQADV 2J3K ASN A  279  UNP  Q39172    ILE   279 CONFLICT                       
SEQADV 2J3K ASN B 1279  UNP  Q39172    ILE   279 CONFLICT                       
SEQRES   1 A  345  MET THR ALA THR ASN LYS GLN VAL ILE LEU LYS ASP TYR          
SEQRES   2 A  345  VAL SER GLY PHE PRO THR GLU SER ASP PHE ASP PHE THR          
SEQRES   3 A  345  THR THR THR VAL GLU LEU ARG VAL PRO GLU GLY THR ASN          
SEQRES   4 A  345  SER VAL LEU VAL LYS ASN LEU TYR LEU SER CYS ASP PRO          
SEQRES   5 A  345  TYR MET ARG ILE ARG MET GLY LYS PRO ASP PRO SER THR          
SEQRES   6 A  345  ALA ALA LEU ALA GLN ALA TYR THR PRO GLY GLN PRO ILE          
SEQRES   7 A  345  GLN GLY TYR GLY VAL SER ARG ILE ILE GLU SER GLY HIS          
SEQRES   8 A  345  PRO ASP TYR LYS LYS GLY ASP LEU LEU TRP GLY ILE VAL          
SEQRES   9 A  345  ALA TRP GLU GLU TYR SER VAL ILE THR PRO MET THR HIS          
SEQRES  10 A  345  ALA HIS PHE LYS ILE GLN HIS THR ASP VAL PRO LEU SER          
SEQRES  11 A  345  TYR TYR THR GLY LEU LEU GLY MET PRO GLY MET THR ALA          
SEQRES  12 A  345  TYR ALA GLY PHE TYR GLU VAL CYS SER PRO LYS GLU GLY          
SEQRES  13 A  345  GLU THR VAL TYR VAL SER ALA ALA SER GLY ALA VAL GLY          
SEQRES  14 A  345  GLN LEU VAL GLY GLN LEU ALA LYS MET MET GLY CYS TYR          
SEQRES  15 A  345  VAL VAL GLY SER ALA GLY SER LYS GLU LYS VAL ASP LEU          
SEQRES  16 A  345  LEU LYS THR LYS PHE GLY PHE ASP ASP ALA PHE ASN TYR          
SEQRES  17 A  345  LYS GLU GLU SER ASP LEU THR ALA ALA LEU LYS ARG CYS          
SEQRES  18 A  345  PHE PRO ASN GLY ILE ASP ILE TYR PHE GLU ASN VAL GLY          
SEQRES  19 A  345  GLY LYS MET LEU ASP ALA VAL LEU VAL ASN MET ASN MET          
SEQRES  20 A  345  HIS GLY ARG ILE ALA VAL CYS GLY MET ILE SER GLN TYR          
SEQRES  21 A  345  ASN LEU GLU ASN GLN GLU GLY VAL HIS ASN LEU SER ASN          
SEQRES  22 A  345  ILE ILE TYR LYS ARG ASN ARG ILE GLN GLY PHE VAL VAL          
SEQRES  23 A  345  SER ASP PHE TYR ASP LYS TYR SER LYS PHE LEU GLU PHE          
SEQRES  24 A  345  VAL LEU PRO HIS ILE ARG GLU GLY LYS ILE THR TYR VAL          
SEQRES  25 A  345  GLU ASP VAL ALA ASP GLY LEU GLU LYS ALA PRO GLU ALA          
SEQRES  26 A  345  LEU VAL GLY LEU PHE HIS GLY LYS ASN VAL GLY LYS GLN          
SEQRES  27 A  345  VAL VAL VAL VAL ALA ARG GLU                                  
SEQRES   1 B  345  MET THR ALA THR ASN LYS GLN VAL ILE LEU LYS ASP TYR          
SEQRES   2 B  345  VAL SER GLY PHE PRO THR GLU SER ASP PHE ASP PHE THR          
SEQRES   3 B  345  THR THR THR VAL GLU LEU ARG VAL PRO GLU GLY THR ASN          
SEQRES   4 B  345  SER VAL LEU VAL LYS ASN LEU TYR LEU SER CYS ASP PRO          
SEQRES   5 B  345  TYR MET ARG ILE ARG MET GLY LYS PRO ASP PRO SER THR          
SEQRES   6 B  345  ALA ALA LEU ALA GLN ALA TYR THR PRO GLY GLN PRO ILE          
SEQRES   7 B  345  GLN GLY TYR GLY VAL SER ARG ILE ILE GLU SER GLY HIS          
SEQRES   8 B  345  PRO ASP TYR LYS LYS GLY ASP LEU LEU TRP GLY ILE VAL          
SEQRES   9 B  345  ALA TRP GLU GLU TYR SER VAL ILE THR PRO MET THR HIS          
SEQRES  10 B  345  ALA HIS PHE LYS ILE GLN HIS THR ASP VAL PRO LEU SER          
SEQRES  11 B  345  TYR TYR THR GLY LEU LEU GLY MET PRO GLY MET THR ALA          
SEQRES  12 B  345  TYR ALA GLY PHE TYR GLU VAL CYS SER PRO LYS GLU GLY          
SEQRES  13 B  345  GLU THR VAL TYR VAL SER ALA ALA SER GLY ALA VAL GLY          
SEQRES  14 B  345  GLN LEU VAL GLY GLN LEU ALA LYS MET MET GLY CYS TYR          
SEQRES  15 B  345  VAL VAL GLY SER ALA GLY SER LYS GLU LYS VAL ASP LEU          
SEQRES  16 B  345  LEU LYS THR LYS PHE GLY PHE ASP ASP ALA PHE ASN TYR          
SEQRES  17 B  345  LYS GLU GLU SER ASP LEU THR ALA ALA LEU LYS ARG CYS          
SEQRES  18 B  345  PHE PRO ASN GLY ILE ASP ILE TYR PHE GLU ASN VAL GLY          
SEQRES  19 B  345  GLY LYS MET LEU ASP ALA VAL LEU VAL ASN MET ASN MET          
SEQRES  20 B  345  HIS GLY ARG ILE ALA VAL CYS GLY MET ILE SER GLN TYR          
SEQRES  21 B  345  ASN LEU GLU ASN GLN GLU GLY VAL HIS ASN LEU SER ASN          
SEQRES  22 B  345  ILE ILE TYR LYS ARG ASN ARG ILE GLN GLY PHE VAL VAL          
SEQRES  23 B  345  SER ASP PHE TYR ASP LYS TYR SER LYS PHE LEU GLU PHE          
SEQRES  24 B  345  VAL LEU PRO HIS ILE ARG GLU GLY LYS ILE THR TYR VAL          
SEQRES  25 B  345  GLU ASP VAL ALA ASP GLY LEU GLU LYS ALA PRO GLU ALA          
SEQRES  26 B  345  LEU VAL GLY LEU PHE HIS GLY LYS ASN VAL GLY LYS GLN          
SEQRES  27 B  345  VAL VAL VAL VAL ALA ARG GLU                                  
HET    NAP  A1346      48                                                       
HET    HNE  A1347      11                                                       
HET    NAP  B2346      48                                                       
HET    HNE  B2347      11                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     HNE (2E,4R)-4-HYDROXYNON-2-ENAL                                      
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  HNE    2(C9 H16 O2)                                                 
FORMUL   7  HOH   *134(H2 O)                                                    
HELIX    1   1 THR A   19  SER A   21  5                                   3    
HELIX    2   2 TYR A   53  MET A   58  1                                   6    
HELIX    3   3 SER A  130  GLY A  134  5                                   5    
HELIX    4   4 GLY A  137  GLU A  149  1                                  13    
HELIX    5   5 VAL A  168  LYS A  177  1                                  10    
HELIX    6   6 SER A  189  LYS A  199  1                                  11    
HELIX    7   7 ASP A  213  PHE A  222  1                                  10    
HELIX    8   8 GLY A  235  ASN A  244  1                                  10    
HELIX    9   9 MET A  256  ASN A  261  1                                   6    
HELIX   10  10 ASN A  270  ILE A  275  5                                   6    
HELIX   11  11 VAL A  285  PHE A  289  5                                   5    
HELIX   12  12 PHE A  289  ASP A  291  5                                   3    
HELIX   13  13 LYS A  292  GLU A  306  1                                  15    
HELIX   14  14 ALA A  322  GLY A  328  1                                   7    
HELIX   15  15 ASP B 1051  ARG B 1057  5                                   7    
HELIX   16  16 PRO B 1128  TYR B 1132  5                                   5    
HELIX   17  17 GLY B 1137  GLU B 1149  1                                  13    
HELIX   18  18 VAL B 1168  ALA B 1176  1                                   9    
HELIX   19  19 SER B 1189  LYS B 1197  1                                   9    
HELIX   20  20 LEU B 1214  PHE B 1222  1                                   9    
HELIX   21  21 GLY B 1235  ASN B 1244  1                                  10    
HELIX   22  22 VAL B 1285  TYR B 1290  5                                   6    
HELIX   23  23 TYR B 1293  ARG B 1305  1                                  13    
HELIX   24  24 LYS B 1321  GLY B 1328  1                                   8    
SHEET    1  AA 2 THR A   2  LEU A  10  0                                        
SHEET    2  AA 2 PHE A  23  GLU A  31 -1  O  ASP A  24   N  ILE A   9           
SHEET    1  AB 5 TYR A 109  ILE A 112  0                                        
SHEET    2  AB 5 VAL A  41  ASN A  45 -1  O  VAL A  41   N  ILE A 112           
SHEET    3  AB 5 GLN A  79  SER A  89 -1  O  ARG A  85   N  LYS A  44           
SHEET    4  AB 5 LEU A  99  ALA A 105 -1  O  LEU A 100   N  SER A  84           
SHEET    5  AB 5 PHE A 120  ILE A 122 -1  O  PHE A 120   N  TRP A 101           
SHEET    1  AC 3 TYR A  47  SER A  49  0                                        
SHEET    2  AC 3 LYS A 337  VAL A 341 -1  O  VAL A 340   N  LEU A  48           
SHEET    3  AC 3 GLU A 313  ASP A 314  1  O  ASP A 314   N  VAL A 339           
SHEET    1  AD12 ASP A 204  ASN A 207  0                                        
SHEET    2  AD12 TYR A 182  ALA A 187  1  O  GLY A 185   N  PHE A 206           
SHEET    3  AD12 THR A 158  SER A 162  1  O  VAL A 159   N  VAL A 184           
SHEET    4  AD12 ILE A 226  GLU A 231  1  N  ASP A 227   O  THR A 158           
SHEET    5  AD12 MET A 245  VAL A 253  1  N  ASN A 246   O  ILE A 226           
SHEET    6  AD12 ARG A 280  GLY A 283  1  O  ARG A 280   N  ILE A 251           
SHEET    7  AD12 ARG B1280  GLY B1283 -1  O  ILE B1281   N  ILE A 281           
SHEET    8  AD12 MET B1245  VAL B1253  1  O  GLY B1249   N  ARG B1280           
SHEET    9  AD12 ILE B1226  GLU B1231  1  O  ILE B1226   N  ASN B1246           
SHEET   10  AD12 THR B1158  VAL B1161  1  O  THR B1158   N  ILE B1228           
SHEET   11  AD12 TYR B1182  ALA B1187  1  O  TYR B1182   N  VAL B1159           
SHEET   12  AD12 ASP B1204  ASN B1207  1  O  ASP B1204   N  GLY B1185           
SHEET    1  BA 2 THR B1002  LEU B1010  0                                        
SHEET    2  BA 2 PHE B1023  GLU B1031 -1  O  ASP B1024   N  ILE B1009           
SHEET    1  BB 5 TYR B1109  ILE B1112  0                                        
SHEET    2  BB 5 VAL B1041  ASN B1045 -1  O  VAL B1041   N  ILE B1112           
SHEET    3  BB 5 GLN B1079  SER B1089 -1  O  ARG B1085   N  LYS B1044           
SHEET    4  BB 5 LEU B1099  ALA B1105 -1  O  LEU B1100   N  SER B1084           
SHEET    5  BB 5 PHE B1120  ILE B1122 -1  O  PHE B1120   N  TRP B1101           
SHEET    1  BC 3 TYR B1047  CYS B1050  0                                        
SHEET    2  BC 3 LYS B1337  VAL B1341 -1  O  GLN B1338   N  CYS B1050           
SHEET    3  BC 3 GLU B1313  ASP B1317  1  O  ASP B1314   N  VAL B1339           
SITE     1 AC1 30 PRO A  52  TYR A  53  MET A 138  THR A 142                    
SITE     2 AC1 30 ALA A 163  SER A 165  GLY A 166  ALA A 167                    
SITE     3 AC1 30 VAL A 168  GLY A 169  ALA A 187  GLY A 188                    
SITE     4 AC1 30 LYS A 192  TYR A 208  ASN A 232  VAL A 233                    
SITE     5 AC1 30 CYS A 254  ILE A 257  SER A 258  TYR A 260                    
SITE     6 AC1 30 PHE A 284  VAL A 285  VAL A 286  LEU A 329                    
SITE     7 AC1 30 PHE A 330  ASN A 334  GLY A 336  HNE A1347                    
SITE     8 AC1 30 HOH A2031  ILE B1275                                          
SITE     1 AC2  5 TYR A  53  MET A 138  TYR A 260  VAL A 286                    
SITE     2 AC2  5 NAP A1346                                                     
SITE     1 AC3 24 PRO B1052  TYR B1053  MET B1138  PRO B1139                    
SITE     2 AC3 24 GLY B1166  ALA B1167  VAL B1168  ALA B1187                    
SITE     3 AC3 24 GLY B1188  LYS B1192  TYR B1208  ASN B1232                    
SITE     4 AC3 24 CYS B1254  GLY B1255  ILE B1257  TYR B1260                    
SITE     5 AC3 24 PHE B1284  VAL B1285  VAL B1286  LEU B1329                    
SITE     6 AC3 24 PHE B1330  HIS B1331  ASN B1334  HNE B2347                    
SITE     1 AC4  7 TYR B1053  LEU B1068  GLN B1070  ILE B1103                    
SITE     2 AC4  7 MET B1138  TYR B1260  NAP B2346                               
CRYST1   49.080  122.450  147.840  90.00  90.00  90.00 P 21 21 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      0.020375  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008167  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006764        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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