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Database: PDB
Entry: 3NAQ
LinkDB: 3NAQ
Original site: 3NAQ 
HEADER    OXIDOREDUCTASE                          02-JUN-10   3NAQ              
TITLE     APO-FORM OF NAD-DEPENDENT FORMATE DEHYDROGENASE FROM HIGHER-PLANT     
TITLE    2 ARABIDOPSIS THALIANA                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FORMATE DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NAD-DEPENDENT FORMATE DEHYDROGENASE, FDH;                   
COMPND   5 EC: 1.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: AT5G14780, FDH, FDH1, T9L3_80;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P1ARAFDH                                  
KEYWDS    NAD-DEPENDENT FORMATE DEHYDROGANASE, HOMODIMER, APO-FORM,             
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.G.SHABALIN,K.M.POLYAKOV,A.E.SEROV,O.E.SKIRGELLO,E.G.SADYKHOV,       
AUTHOR   2 P.V.DOROVATOVSKIY,V.I.TISHKOV,V.O.POPOV                              
REVDAT   1   07-JUL-10 3NAQ    0                                                
JRNL        AUTH   I.G.SHABALIN,K.M.POLYAKOV,O.E.SKIRGELLO,V.I.TISHKOV,         
JRNL        AUTH 2 V.O.POPOV                                                    
JRNL        TITL   STRUCTURES OF THE APO AND HOLO FORMS OF NAD-DEPENDENT        
JRNL        TITL 2 FORMATE DEHYDROGENASE FROM THE HIGHER-PLANT ARABIDOPSIS      
JRNL        TITL 3 THALIANA                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0070                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 83414                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4407                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6006                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 322                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 559                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.05000                                             
REMARK   3    B22 (A**2) : 1.90000                                              
REMARK   3    B33 (A**2) : 1.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.093         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.563         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5580 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3730 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7568 ; 1.589 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9132 ; 0.977 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   700 ; 6.314 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;32.784 ;24.426       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   954 ;13.925 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;20.182 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   836 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6202 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1070 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3484 ; 0.886 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1428 ; 0.304 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5603 ; 1.470 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2096 ; 2.418 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1965 ; 3.731 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    28        A   145                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.9090  -1.0580   6.0160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1836 T22:   0.0331                                     
REMARK   3      T33:   0.0923 T12:  -0.0015                                     
REMARK   3      T13:   0.0084 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2544 L22:   1.5525                                     
REMARK   3      L33:   1.1155 L12:  -0.3913                                     
REMARK   3      L13:  -0.3116 L23:   0.8665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0312 S12:   0.0751 S13:   0.1612                       
REMARK   3      S21:  -0.1701 S22:   0.0278 S23:  -0.0255                       
REMARK   3      S31:  -0.1064 S32:   0.0175 S33:  -0.0590                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   146        A   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6300  -2.1510  11.7430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1504 T22:   0.2170                                     
REMARK   3      T33:   0.1207 T12:  -0.0473                                     
REMARK   3      T13:   0.0401 T23:  -0.1358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9173 L22:   1.0893                                     
REMARK   3      L33:   0.8801 L12:  -0.3562                                     
REMARK   3      L13:  -0.4350 L23:   0.0505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1956 S12:   0.9378 S13:  -0.4710                       
REMARK   3      S21:  -0.0929 S22:   0.0319 S23:   0.0297                       
REMARK   3      S31:   0.1310 S32:  -0.1506 S33:   0.1637                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   333        A   378                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4790 -10.6820  14.3700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2083 T22:   0.0681                                     
REMARK   3      T33:   0.1356 T12:  -0.0061                                     
REMARK   3      T13:   0.0066 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3096 L22:   1.2234                                     
REMARK   3      L33:   0.9854 L12:  -0.0475                                     
REMARK   3      L13:  -0.1988 L23:   0.2913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0534 S12:  -0.1700 S13:  -0.0695                       
REMARK   3      S21:   0.0294 S22:   0.0367 S23:  -0.0035                       
REMARK   3      S31:   0.1575 S32:  -0.0210 S33:   0.0167                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    28        B   145                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3150  20.5650  27.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1810 T22:   0.0465                                     
REMARK   3      T33:   0.0755 T12:   0.0071                                     
REMARK   3      T13:  -0.0006 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2227 L22:   1.2871                                     
REMARK   3      L33:   1.6217 L12:  -0.3087                                     
REMARK   3      L13:  -0.3362 L23:   0.9428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0290 S12:   0.1552 S13:   0.0719                       
REMARK   3      S21:  -0.1235 S22:  -0.0529 S23:   0.0053                       
REMARK   3      S31:  -0.1851 S32:  -0.0117 S33:   0.0239                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   146        B   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8760  14.8040  28.7320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.0806                                     
REMARK   3      T33:   0.2687 T12:   0.0395                                     
REMARK   3      T13:  -0.0477 T23:  -0.1369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8378 L22:   0.8267                                     
REMARK   3      L33:   1.1733 L12:  -0.5239                                     
REMARK   3      L13:  -0.3311 L23:   0.0853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1939 S12:  -0.4831 S13:   0.9408                       
REMARK   3      S21:   0.1185 S22:   0.1535 S23:  -0.1429                       
REMARK   3      S31:  -0.0959 S32:   0.0301 S33:   0.0403                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   333        B   378                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8920  12.1910  37.3470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1969 T22:   0.0750                                     
REMARK   3      T33:   0.1040 T12:   0.0071                                     
REMARK   3      T13:  -0.0094 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6831 L22:   1.0569                                     
REMARK   3      L33:   1.2739 L12:  -0.2229                                     
REMARK   3      L13:  -0.2380 L23:   0.3429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0268 S12:  -0.0629 S13:  -0.1934                       
REMARK   3      S21:   0.1736 S22:   0.0090 S23:  -0.0424                       
REMARK   3      S31:   0.0309 S32:   0.0009 S33:   0.0178                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3NAQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059593.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.81                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.2500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.360                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (2UL): 6 MG/ML FDH,     
REMARK 280  0.1M NA2HPO4, PH 7.0, 10 MM EDTA. RESERVOIR SOLUTION (2UL): 0.1M    
REMARK 280  BIS-TRIS, PH 6.0, 2.1M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING   
REMARK 280  DROP, TEMPERATURE 293K                                              
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       35.16500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.11500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.16500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.11500            
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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     PHE A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     PHE B    22                                                      
REMARK 465     ASN B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  77    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  80    CG   OD1  OD2                                       
REMARK 470     GLU A 228    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 231    CD   CE   NZ                                        
REMARK 470     LYS A 236    CE   NZ                                             
REMARK 470     ASN A 242    OD1  ND2                                            
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     LYS A 267    CD   CE   NZ                                        
REMARK 470     GLU B  77    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 228    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 231    CD   CE   NZ                                        
REMARK 470     LYS B 236    CE   NZ                                             
REMARK 470     ASN B 242    OD1  ND2                                            
REMARK 470     LYS B 247    CE   NZ                                             
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     LYS B 267    CD   CE   NZ                                        
REMARK 470     GLU B 268    CD   OE1  OE2                                       
REMARK 470     LYS B 272    CE   NZ                                             
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  40     -127.49     52.24                                   
REMARK 500    HIS A  99       66.23   -162.20                                   
REMARK 500    ALA A 199       53.96   -149.07                                   
REMARK 500    ASN A 254       46.70   -140.62                                   
REMARK 500    ALA A 283      -83.91    -94.87                                   
REMARK 500    ASN B  40     -128.69     51.49                                   
REMARK 500    HIS B  99       65.44   -159.68                                   
REMARK 500    ALA B 199       55.79   -148.11                                   
REMARK 500    ASN B 254       44.17   -140.95                                   
REMARK 500    ALA B 283      -82.64    -96.90                                   
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 B 644        DISTANCE =  5.58 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 18                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 20                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 19                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N7U   RELATED DB: PDB                                   
REMARK 900 FDH FROM ARABIDOPSIS THALIANA IN HOLO-FORM                           
REMARK 900 RELATED ID: 2GSD   RELATED DB: PDB                                   
REMARK 900 FDH FROM MORAXELLA SP.C-1 IN HOLO-FORM                               
REMARK 900 RELATED ID: 3FN4   RELATED DB: PDB                                   
REMARK 900 FDH FROM MORAXELLA SP.C-1 IN APO-FORM IN CLOSED CONFORMATION         
REMARK 900 RELATED ID: 2NAD   RELATED DB: PDB                                   
REMARK 900 FDH FROM PSEUDOMONAS SP.101 IN HOLO-FORM                             
REMARK 900 RELATED ID: 2NAC   RELATED DB: PDB                                   
REMARK 900 FDH FROM PSEUDOMONAS SP.101 IN APO-FORM                              
REMARK 900 RELATED ID: 2FSS   RELATED DB: PDB                                   
REMARK 900 FDH FROM CANDIDA BOIDINII IN APO-FORM                                
DBREF  3NAQ A   22   378  UNP    Q9S7E4   FDH_ARATH       28    384             
DBREF  3NAQ B   22   378  UNP    Q9S7E4   FDH_ARATH       28    384             
SEQRES   1 A  357  PHE ASN ALA SER SER GLY ASP SER LYS LYS ILE VAL GLY          
SEQRES   2 A  357  VAL PHE TYR LYS ALA ASN GLU TYR ALA THR LYS ASN PRO          
SEQRES   3 A  357  ASN PHE LEU GLY CYS VAL GLU ASN ALA LEU GLY ILE ARG          
SEQRES   4 A  357  ASP TRP LEU GLU SER GLN GLY HIS GLN TYR ILE VAL THR          
SEQRES   5 A  357  ASP ASP LYS GLU GLY PRO ASP CYS GLU LEU GLU LYS HIS          
SEQRES   6 A  357  ILE PRO ASP LEU HIS VAL LEU ILE SER THR PRO PHE HIS          
SEQRES   7 A  357  PRO ALA TYR VAL THR ALA GLU ARG ILE LYS LYS ALA LYS          
SEQRES   8 A  357  ASN LEU LYS LEU LEU LEU THR ALA GLY ILE GLY SER ASP          
SEQRES   9 A  357  HIS ILE ASP LEU GLN ALA ALA ALA ALA ALA GLY LEU THR          
SEQRES  10 A  357  VAL ALA GLU VAL THR GLY SER ASN VAL VAL SER VAL ALA          
SEQRES  11 A  357  GLU ASP GLU LEU MET ARG ILE LEU ILE LEU MET ARG ASN          
SEQRES  12 A  357  PHE VAL PRO GLY TYR ASN GLN VAL VAL LYS GLY GLU TRP          
SEQRES  13 A  357  ASN VAL ALA GLY ILE ALA TYR ARG ALA TYR ASP LEU GLU          
SEQRES  14 A  357  GLY LYS THR ILE GLY THR VAL GLY ALA GLY ARG ILE GLY          
SEQRES  15 A  357  LYS LEU LEU LEU GLN ARG LEU LYS PRO PHE GLY CYS ASN          
SEQRES  16 A  357  LEU LEU TYR HIS ASP ARG LEU GLN MET ALA PRO GLU LEU          
SEQRES  17 A  357  GLU LYS GLU THR GLY ALA LYS PHE VAL GLU ASP LEU ASN          
SEQRES  18 A  357  GLU MET LEU PRO LYS CYS ASP VAL ILE VAL ILE ASN MET          
SEQRES  19 A  357  PRO LEU THR GLU LYS THR ARG GLY MET PHE ASN LYS GLU          
SEQRES  20 A  357  LEU ILE GLY LYS LEU LYS LYS GLY VAL LEU ILE VAL ASN          
SEQRES  21 A  357  ASN ALA ARG GLY ALA ILE MET GLU ARG GLN ALA VAL VAL          
SEQRES  22 A  357  ASP ALA VAL GLU SER GLY HIS ILE GLY GLY TYR SER GLY          
SEQRES  23 A  357  ASP VAL TRP ASP PRO GLN PRO ALA PRO LYS ASP HIS PRO          
SEQRES  24 A  357  TRP ARG TYR MET PRO ASN GLN ALA MET THR PRO HIS THR          
SEQRES  25 A  357  SER GLY THR THR ILE ASP ALA GLN LEU ARG TYR ALA ALA          
SEQRES  26 A  357  GLY THR LYS ASP MET LEU GLU ARG TYR PHE LYS GLY GLU          
SEQRES  27 A  357  ASP PHE PRO THR GLU ASN TYR ILE VAL LYS ASP GLY GLU          
SEQRES  28 A  357  LEU ALA PRO GLN TYR ARG                                      
SEQRES   1 B  357  PHE ASN ALA SER SER GLY ASP SER LYS LYS ILE VAL GLY          
SEQRES   2 B  357  VAL PHE TYR LYS ALA ASN GLU TYR ALA THR LYS ASN PRO          
SEQRES   3 B  357  ASN PHE LEU GLY CYS VAL GLU ASN ALA LEU GLY ILE ARG          
SEQRES   4 B  357  ASP TRP LEU GLU SER GLN GLY HIS GLN TYR ILE VAL THR          
SEQRES   5 B  357  ASP ASP LYS GLU GLY PRO ASP CYS GLU LEU GLU LYS HIS          
SEQRES   6 B  357  ILE PRO ASP LEU HIS VAL LEU ILE SER THR PRO PHE HIS          
SEQRES   7 B  357  PRO ALA TYR VAL THR ALA GLU ARG ILE LYS LYS ALA LYS          
SEQRES   8 B  357  ASN LEU LYS LEU LEU LEU THR ALA GLY ILE GLY SER ASP          
SEQRES   9 B  357  HIS ILE ASP LEU GLN ALA ALA ALA ALA ALA GLY LEU THR          
SEQRES  10 B  357  VAL ALA GLU VAL THR GLY SER ASN VAL VAL SER VAL ALA          
SEQRES  11 B  357  GLU ASP GLU LEU MET ARG ILE LEU ILE LEU MET ARG ASN          
SEQRES  12 B  357  PHE VAL PRO GLY TYR ASN GLN VAL VAL LYS GLY GLU TRP          
SEQRES  13 B  357  ASN VAL ALA GLY ILE ALA TYR ARG ALA TYR ASP LEU GLU          
SEQRES  14 B  357  GLY LYS THR ILE GLY THR VAL GLY ALA GLY ARG ILE GLY          
SEQRES  15 B  357  LYS LEU LEU LEU GLN ARG LEU LYS PRO PHE GLY CYS ASN          
SEQRES  16 B  357  LEU LEU TYR HIS ASP ARG LEU GLN MET ALA PRO GLU LEU          
SEQRES  17 B  357  GLU LYS GLU THR GLY ALA LYS PHE VAL GLU ASP LEU ASN          
SEQRES  18 B  357  GLU MET LEU PRO LYS CYS ASP VAL ILE VAL ILE ASN MET          
SEQRES  19 B  357  PRO LEU THR GLU LYS THR ARG GLY MET PHE ASN LYS GLU          
SEQRES  20 B  357  LEU ILE GLY LYS LEU LYS LYS GLY VAL LEU ILE VAL ASN          
SEQRES  21 B  357  ASN ALA ARG GLY ALA ILE MET GLU ARG GLN ALA VAL VAL          
SEQRES  22 B  357  ASP ALA VAL GLU SER GLY HIS ILE GLY GLY TYR SER GLY          
SEQRES  23 B  357  ASP VAL TRP ASP PRO GLN PRO ALA PRO LYS ASP HIS PRO          
SEQRES  24 B  357  TRP ARG TYR MET PRO ASN GLN ALA MET THR PRO HIS THR          
SEQRES  25 B  357  SER GLY THR THR ILE ASP ALA GLN LEU ARG TYR ALA ALA          
SEQRES  26 B  357  GLY THR LYS ASP MET LEU GLU ARG TYR PHE LYS GLY GLU          
SEQRES  27 B  357  ASP PHE PRO THR GLU ASN TYR ILE VAL LYS ASP GLY GLU          
SEQRES  28 B  357  LEU ALA PRO GLN TYR ARG                                      
HET    SO4  A   1       5                                                       
HET    SO4  A  18       5                                                       
HET    SO4  A  20       5                                                       
HET    SO4  B   2       5                                                       
HET    SO4  B   3       5                                                       
HET    SO4  B  19       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  HOH   *559(H2 O)                                                    
HELIX    1   1 ASN A   40  ASN A   46  1                                   7    
HELIX    2   2 ASN A   55  GLY A   58  5                                   4    
HELIX    3   3 ILE A   59  GLN A   66  1                                   8    
HELIX    4   4 CYS A   81  ILE A   87  1                                   7    
HELIX    5   5 THR A  104  ALA A  111  1                                   8    
HELIX    6   6 ASP A  128  ALA A  135  1                                   8    
HELIX    7   7 ASN A  146  ASN A  164  1                                  19    
HELIX    8   8 ASN A  164  GLY A  175  1                                  12    
HELIX    9   9 VAL A  179  TYR A  184  1                                   6    
HELIX   10  10 GLY A  200  LYS A  211  1                                  12    
HELIX   11  11 PRO A  212  GLY A  214  5                                   3    
HELIX   12  12 ALA A  226  GLY A  234  1                                   9    
HELIX   13  13 ASP A  240  LEU A  245  1                                   6    
HELIX   14  14 PRO A  246  CYS A  248  5                                   3    
HELIX   15  15 ASN A  266  LEU A  273  1                                   8    
HELIX   16  16 ARG A  284  MET A  288  5                                   5    
HELIX   17  17 GLU A  289  SER A  299  1                                  11    
HELIX   18  18 HIS A  319  TYR A  323  5                                   5    
HELIX   19  19 THR A  337  GLY A  358  1                                  22    
HELIX   20  20 PRO A  362  GLU A  364  5                                   3    
HELIX   21  21 PRO A  375  ARG A  378  5                                   4    
HELIX   22  22 ASN B   40  ASN B   46  1                                   7    
HELIX   23  23 ASN B   55  GLY B   58  5                                   4    
HELIX   24  24 ILE B   59  GLN B   66  1                                   8    
HELIX   25  25 CYS B   81  ILE B   87  1                                   7    
HELIX   26  26 THR B  104  ALA B  111  1                                   8    
HELIX   27  27 ASP B  128  ALA B  135  1                                   8    
HELIX   28  28 ASN B  146  ASN B  164  1                                  19    
HELIX   29  29 ASN B  164  GLY B  175  1                                  12    
HELIX   30  30 VAL B  179  TYR B  184  1                                   6    
HELIX   31  31 GLY B  200  LYS B  211  1                                  12    
HELIX   32  32 PRO B  212  GLY B  214  5                                   3    
HELIX   33  33 ALA B  226  GLY B  234  1                                   9    
HELIX   34  34 ASP B  240  LEU B  245  1                                   6    
HELIX   35  35 PRO B  246  CYS B  248  5                                   3    
HELIX   36  36 ASN B  266  LEU B  273  1                                   8    
HELIX   37  37 ARG B  284  MET B  288  5                                   5    
HELIX   38  38 GLU B  289  SER B  299  1                                  11    
HELIX   39  39 HIS B  319  TYR B  323  5                                   5    
HELIX   40  40 THR B  337  GLY B  358  1                                  22    
HELIX   41  41 PRO B  362  GLU B  364  5                                   3    
HELIX   42  42 PRO B  375  ARG B  378  5                                   4    
SHEET    1   A 7 GLN A  69  THR A  73  0                                        
SHEET    2   A 7 LYS A  31  VAL A  35  1  N  ILE A  32   O  GLN A  69           
SHEET    3   A 7 VAL A  92  SER A  95  1  O  ILE A  94   N  VAL A  35           
SHEET    4   A 7 LEU A 116  THR A 119  1  O  LEU A 116   N  LEU A  93           
SHEET    5   A 7 THR A 138  GLU A 141  1  O  THR A 138   N  LEU A 117           
SHEET    6   A 7 TYR A 366  LYS A 369 -1  O  ILE A 367   N  VAL A 139           
SHEET    7   A 7 GLU A 372  LEU A 373 -1  O  GLU A 372   N  LYS A 369           
SHEET    1   B 6 LYS A 236  PHE A 237  0                                        
SHEET    2   B 6 ASN A 216  HIS A 220  1  N  LEU A 217   O  LYS A 236           
SHEET    3   B 6 THR A 193  VAL A 197  1  N  ILE A 194   O  LEU A 218           
SHEET    4   B 6 VAL A 250  ILE A 253  1  O  VAL A 252   N  VAL A 197           
SHEET    5   B 6 VAL A 277  ASN A 281  1  O  LEU A 278   N  ILE A 251           
SHEET    6   B 6 ILE A 302  GLY A 307  1  O  SER A 306   N  ASN A 281           
SHEET    1   C 7 GLN B  69  THR B  73  0                                        
SHEET    2   C 7 LYS B  31  VAL B  35  1  N  ILE B  32   O  GLN B  69           
SHEET    3   C 7 VAL B  92  SER B  95  1  O  ILE B  94   N  VAL B  33           
SHEET    4   C 7 LEU B 116  THR B 119  1  O  LEU B 116   N  LEU B  93           
SHEET    5   C 7 THR B 138  GLU B 141  1  O  THR B 138   N  LEU B 117           
SHEET    6   C 7 TYR B 366  LYS B 369 -1  O  ILE B 367   N  VAL B 139           
SHEET    7   C 7 GLU B 372  LEU B 373 -1  O  GLU B 372   N  LYS B 369           
SHEET    1   D 6 LYS B 236  PHE B 237  0                                        
SHEET    2   D 6 ASN B 216  HIS B 220  1  N  LEU B 217   O  LYS B 236           
SHEET    3   D 6 THR B 193  VAL B 197  1  N  ILE B 194   O  LEU B 218           
SHEET    4   D 6 VAL B 250  ILE B 253  1  O  VAL B 252   N  VAL B 197           
SHEET    5   D 6 VAL B 277  ASN B 281  1  O  LEU B 278   N  ILE B 251           
SHEET    6   D 6 ILE B 302  GLY B 307  1  O  GLY B 304   N  ILE B 279           
CISPEP   1 ASP A  311    PRO A  312          0        -5.67                     
CISPEP   2 GLN A  313    PRO A  314          0        -4.50                     
CISPEP   3 ASP B  311    PRO B  312          0        -1.77                     
CISPEP   4 GLN B  313    PRO B  314          0        -2.98                     
SITE     1 AC1  4 ARG A 354  PRO A 362  HOH A 396  HOH A 479                    
SITE     1 AC2  4 GLU A 359  ASP A 360  HOH A 418  HOH A 581                    
SITE     1 AC3  3 TYR A 184  ARG A 185  LYS B  45                               
SITE     1 AC4  3 ARG B 354  HOH B 432  HOH B 549                               
SITE     1 AC5  3 GLU B 359  ASP B 360  HOH B 455                               
SITE     1 AC6  4 TYR B 184  ARG B 185  ASN B 326  HOH B 558                    
CRYST1   70.330  106.230  106.500  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      0.014219  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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