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Database: PDB
Entry: 2JJY
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Original site: 2JJY 
HEADER    OXIDOREDUCTASE                          25-APR-08   2JJY              
TITLE     CRYSTAL STRUCTURE OF FRANCISELLA TULARENSIS ENOYL REDUCTASE           
TITLE    2 (FTFABI) WITH BOUND NAD                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE;                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ENOYL REDUCTASE, NADH;                                      
COMPND   5 EC: 1.3.1.9;                                                         
COMPND   6 OTHER_DETAILS: 6XHISTIDINE AT C-TERMINUS                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS;                         
SOURCE   3 ORGANISM_TAXID: 263                                                  
KEYWDS    OXIDOREDUCTASE, FATTY ACID BIOSYNTHESIS                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.R.LUCKNER,H.LU,J.J.TRUGLIO,P.J.TONGE,C.KISKER                       
REVDAT   3   13-JUL-11 2JJY    1       VERSN                                    
REVDAT   2   23-JUN-09 2JJY    1       JRNL                                     
REVDAT   1   24-FEB-09 2JJY    0                                                
JRNL        AUTH   H.LU,K.ENGLAND,C.AM ENDE,J.J.TRUGLIO,S.R.LUCKNER,N.MARLENEE, 
JRNL        AUTH 2 S.E.KNUDSON,D.L.KNUDSON,R.A.BOWEN,C.KISKER,R.A.SLAYDEN,      
JRNL        AUTH 3 P.J.TONGE                                                    
JRNL        TITL   SLOW-ONSET INHIBITION OF THE FABI ENOYL REDUCTASE FROM       
JRNL        TITL 2 FRANCISELLA TULARENSIS: RESIDENCE TIME AND IN VIVO ACTIVITY  
JRNL        REF    ACS CHEM.BIOL.                V.   4   221 2009              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   19206187                                                     
JRNL        DOI    10.1021/CB800306Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019 24/04/2001                           
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24222                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1231                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1620                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.259                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.355                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7536                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : 49.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.03                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89700                                              
REMARK   3    B22 (A**2) : 0.24400                                              
REMARK   3    B33 (A**2) : -1.14100                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.476         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.345         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.833        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.826                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7712 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10423 ; 1.551 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   995 ; 7.028 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   307 ;38.776 ;24.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1311 ;19.868 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;20.572 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1202 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5687 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3808 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5315 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   286 ; 0.144 ; 0.200       
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):    24 ; 0.158 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.431 ; 0.200       
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):  5057 ; 0.417 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7875 ; 0.697 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2973 ; 0.985 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2547 ; 1.551 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     190      4                      
REMARK   3           1     B      2       B     190      4                      
REMARK   3           1     C      2       C     190      4                      
REMARK   3           1     D      2       D     190      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1417 ;  0.38 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1417 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1417 ;  0.38 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1417 ;  0.44 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1417 ;  0.51 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1417 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1417 ;  0.49 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1417 ;  0.48 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    210       A     256      4                      
REMARK   3           1     B    210       B     256      4                      
REMARK   3           1     C    210       C     256      4                      
REMARK   3           1     D    210       D     256      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    328 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    328 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    328 ;  0.41 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    328 ;  0.34 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    328 ;  0.51 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    328 ;  0.50 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    328 ;  0.61 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    328 ;  0.54 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS : 4                                           
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     2        A   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5150  -6.1323  -0.8280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0945 T22:  -0.0605                                     
REMARK   3      T33:  -0.0779 T12:   0.0229                                     
REMARK   3      T13:  -0.0012 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9283 L22:   1.0792                                     
REMARK   3      L33:   1.4539 L12:  -0.1175                                     
REMARK   3      L13:  -0.8982 L23:  -0.6753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0612 S12:   0.1954 S13:  -0.1021                       
REMARK   3      S21:  -0.1361 S22:   0.0605 S23:  -0.0083                       
REMARK   3      S31:   0.0680 S32:  -0.0057 S33:   0.0007                       
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 :   B     2        B   263                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.2714  16.8208   6.4740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0002 T22:  -0.1097                                     
REMARK   3      T33:  -0.0771 T12:   0.0238                                     
REMARK   3      T13:  -0.0091 T23:  -0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8174 L22:   1.5612                                     
REMARK   3      L33:   0.9180 L12:   0.0952                                     
REMARK   3      L13:  -0.6450 L23:  -0.2864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0238 S12:  -0.0861 S13:   0.2121                       
REMARK   3      S21:   0.1765 S22:   0.0115 S23:   0.0442                       
REMARK   3      S31:  -0.3793 S32:   0.0052 S33:  -0.0353                       
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 :   C     2        C   268                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.8863  -6.2226  15.0483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0929 T22:  -0.0397                                     
REMARK   3      T33:  -0.0743 T12:   0.0143                                     
REMARK   3      T13:  -0.0345 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3429 L22:   1.5385                                     
REMARK   3      L33:   1.1829 L12:   0.0380                                     
REMARK   3      L13:  -0.4821 L23:  -0.5856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:   0.2351 S13:  -0.0511                       
REMARK   3      S21:  -0.1392 S22:   0.0145 S23:   0.1388                       
REMARK   3      S31:   0.0460 S32:  -0.3380 S33:   0.0084                       
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 :   D     2        D   260                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4058 -22.6883  22.6828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0581 T22:  -0.1088                                     
REMARK   3      T33:  -0.0923 T12:   0.0427                                     
REMARK   3      T13:  -0.0143 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6542 L22:   1.1673                                     
REMARK   3      L33:   1.5282 L12:   0.2353                                     
REMARK   3      L13:  -0.6079 L23:  -0.5264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:  -0.1067 S13:  -0.1120                       
REMARK   3      S21:   0.2146 S22:  -0.0781 S23:  -0.1673                       
REMARK   3      S31:   0.0369 S32:   0.1557 S33:   0.0735                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL PLUS 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   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. RESIDUES A194 - A204 DISORDERED; RESIDUES         
REMARK   3  B196 - B211 DISORDERED; RESIDUES C193 - C207 DISORDERED;            
REMARK   3  RESIDUES D193 - C204 DISORDERED; ADDITIONAL RESIDUES AT C-          
REMARK   3  TERMINUS OF CHAIN A, B, C FROM 6XHISTIDINE TAG.                     
REMARK   4                                                                      
REMARK   4 2JJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-APR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-36034.                                       
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                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10500                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24222                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.32                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.2                                
REMARK 200  R MERGE                    (I) : 0.18                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MG ACETATE.                    
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       48.00300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.51600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.72700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.51600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.00300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.72700            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.6 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A   194                                                      
REMARK 465     LEU A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     ILE A   200                                                      
REMARK 465     SER A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     PHE A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     ILE B   200                                                      
REMARK 465     SER B   201                                                      
REMARK 465     ASN B   202                                                      
REMARK 465     PHE B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     MET B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     TYR B   209                                                      
REMARK 465     ASN B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     HIS B   264                                                      
REMARK 465     HIS B   265                                                      
REMARK 465     HIS B   266                                                      
REMARK 465     HIS B   267                                                      
REMARK 465     HIS B   268                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C   193                                                      
REMARK 465     THR C   194                                                      
REMARK 465     LEU C   195                                                      
REMARK 465     ALA C   196                                                      
REMARK 465     ALA C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     GLY C   199                                                      
REMARK 465     ILE C   200                                                      
REMARK 465     SER C   201                                                      
REMARK 465     ASN C   202                                                      
REMARK 465     PHE C   203                                                      
REMARK 465     LYS C   204                                                      
REMARK 465     LYS C   205                                                      
REMARK 465     MET C   206                                                      
REMARK 465     LEU C   207                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D   193                                                      
REMARK 465     THR D   194                                                      
REMARK 465     LEU D   195                                                      
REMARK 465     ALA D   196                                                      
REMARK 465     ALA D   197                                                      
REMARK 465     SER D   198                                                      
REMARK 465     GLY D   199                                                      
REMARK 465     ILE D   200                                                      
REMARK 465     SER D   201                                                      
REMARK 465     ASN D   202                                                      
REMARK 465     PHE D   203                                                      
REMARK 465     LYS D   204                                                      
REMARK 465     LEU D   261                                                      
REMARK 465     GLU D   262                                                      
REMARK 465     HIS D   263                                                      
REMARK 465     HIS D   264                                                      
REMARK 465     HIS D   265                                                      
REMARK 465     HIS D   266                                                      
REMARK 465     HIS D   267                                                      
REMARK 465     HIS D   268                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 144   CA  -  CB  -  CG  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    CYS C  62   CA  -  CB  -  SG  ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    LEU D 144   CA  -  CB  -  CG  ANGL. DEV. = -14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  55       70.00     41.48                                   
REMARK 500    GLU A 100       77.51   -117.18                                   
REMARK 500    ALA A 120      -60.60   -130.00                                   
REMARK 500    ARG A 137       34.15   -154.62                                   
REMARK 500    SER A 155      -38.91     72.98                                   
REMARK 500    ASN A 157     -115.87     52.36                                   
REMARK 500    MET A 206       77.13   -112.62                                   
REMARK 500    THR A 238        0.19    -65.24                                   
REMARK 500    VAL A 247       79.98   -101.32                                   
REMARK 500    ASP A 248       25.22   -141.14                                   
REMARK 500    GLN B  42       32.95    -80.86                                   
REMARK 500    ASN B  55       66.54     39.09                                   
REMARK 500    CYS B  62       94.20   -169.02                                   
REMARK 500    SER B  90       69.76   -115.68                                   
REMARK 500    ALA B 120      -60.22   -105.91                                   
REMARK 500    ARG B 137       31.15   -165.48                                   
REMARK 500    SER B 155      -31.54     52.38                                   
REMARK 500    ASN B 157     -125.58     39.52                                   
REMARK 500    GLU B 179        3.04    -61.43                                   
REMARK 500    ASP B 248       21.36   -144.54                                   
REMARK 500    ALA C  52      -29.24    -38.31                                   
REMARK 500    ASN C  55       67.93     35.20                                   
REMARK 500    VAL C  64        4.48    -68.76                                   
REMARK 500    ALA C 120      -56.36   -121.56                                   
REMARK 500    SER C 122      -29.04    -38.66                                   
REMARK 500    ASN C 136       70.36     46.74                                   
REMARK 500    ARG C 137       36.02   -153.58                                   
REMARK 500    ILE C 147      -17.28    -48.25                                   
REMARK 500    SER C 155      -20.71     69.26                                   
REMARK 500    ASN C 157     -121.93     17.29                                   
REMARK 500    VAL C 247       78.84   -107.30                                   
REMARK 500    ASP C 248       41.57   -142.89                                   
REMARK 500    ALA C 249       18.93     49.40                                   
REMARK 500    MET C 256       10.45   -140.98                                   
REMARK 500    ASN D  17      -32.55    -38.66                                   
REMARK 500    ALA D  33     -178.43    -66.71                                   
REMARK 500    GLN D  42       30.98    -98.60                                   
REMARK 500    VAL D  64       10.02    -64.20                                   
REMARK 500    SER D  90       69.85   -117.56                                   
REMARK 500    PHE D  93      138.46   -171.27                                   
REMARK 500    VAL D 107      131.65    -35.00                                   
REMARK 500    ALA D 120      -61.35   -128.64                                   
REMARK 500    ARG D 137       20.04   -153.44                                   
REMARK 500    SER D 155       -3.65     41.94                                   
REMARK 500    ASN D 157     -138.52     52.23                                   
REMARK 500    VAL D 247       72.88   -112.23                                   
REMARK 500    ASP D 248       36.33   -140.24                                   
REMARK 500    ALA D 249        3.86     56.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER C 155        23.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D1261                 
DBREF  2JJY A    1   260  UNP    Q14I55   Q14I55_FRAT1     1    260             
DBREF  2JJY B    1   260  UNP    Q14I55   Q14I55_FRAT1     1    260             
DBREF  2JJY C    1   260  UNP    Q14I55   Q14I55_FRAT1     1    260             
DBREF  2JJY D    1   260  UNP    Q14I55   Q14I55_FRAT1     1    260             
SEQADV 2JJY LEU A  261  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY GLU A  262  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  263  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  264  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  265  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  266  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  267  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS A  268  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY LEU B  261  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY GLU B  262  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  263  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  264  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  265  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  266  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  267  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS B  268  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY LEU C  261  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY GLU C  262  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  263  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  264  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  265  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  266  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  267  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS C  268  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY LEU D  261  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY GLU D  262  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  263  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  264  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  265  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  266  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  267  UNP  Q14I55              EXPRESSION TAG                 
SEQADV 2JJY HIS D  268  UNP  Q14I55              EXPRESSION TAG                 
SEQRES   1 A  268  MET GLY PHE LEU ALA GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 A  268  LEU LEU SER ASN LYS SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 A  268  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 A  268  VAL GLY GLN PHE LYS ASP ARG VAL GLU LYS LEU CYS ALA          
SEQRES   5 A  268  GLU PHE ASN PRO ALA ALA VAL LEU PRO CYS ASP VAL ILE          
SEQRES   6 A  268  SER ASP GLN GLU ILE LYS ASP LEU PHE VAL GLU LEU GLY          
SEQRES   7 A  268  LYS VAL TRP ASP GLY LEU ASP ALA ILE VAL HIS SER ILE          
SEQRES   8 A  268  ALA PHE ALA PRO ARG ASP GLN LEU GLU GLY ASN PHE ILE          
SEQRES   9 A  268  ASP CYS VAL THR ARG GLU GLY PHE SER ILE ALA HIS ASP          
SEQRES  10 A  268  ILE SER ALA TYR SER PHE ALA ALA LEU ALA LYS GLU GLY          
SEQRES  11 A  268  ARG SER MET MET LYS ASN ARG ASN ALA SER MET VAL ALA          
SEQRES  12 A  268  LEU THR TYR ILE GLY ALA GLU LYS ALA MET PRO SER TYR          
SEQRES  13 A  268  ASN THR MET GLY VAL ALA LYS ALA SER LEU GLU ALA THR          
SEQRES  14 A  268  VAL ARG TYR THR ALA LEU ALA LEU GLY GLU ASP GLY ILE          
SEQRES  15 A  268  LYS VAL ASN ALA VAL SER ALA GLY PRO ILE LYS THR LEU          
SEQRES  16 A  268  ALA ALA SER GLY ILE SER ASN PHE LYS LYS MET LEU ASP          
SEQRES  17 A  268  TYR ASN ALA MET VAL SER PRO LEU LYS LYS ASN VAL ASP          
SEQRES  18 A  268  ILE MET GLU VAL GLY ASN THR VAL ALA PHE LEU CYS SER          
SEQRES  19 A  268  ASP MET ALA THR GLY ILE THR GLY GLU VAL VAL HIS VAL          
SEQRES  20 A  268  ASP ALA GLY TYR HIS CYS VAL SER MET GLY ASN VAL LEU          
SEQRES  21 A  268  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  268  MET GLY PHE LEU ALA GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 B  268  LEU LEU SER ASN LYS SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 B  268  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 B  268  VAL GLY GLN PHE LYS ASP ARG VAL GLU LYS LEU CYS ALA          
SEQRES   5 B  268  GLU PHE ASN PRO ALA ALA VAL LEU PRO CYS ASP VAL ILE          
SEQRES   6 B  268  SER ASP GLN GLU ILE LYS ASP LEU PHE VAL GLU LEU GLY          
SEQRES   7 B  268  LYS VAL TRP ASP GLY LEU ASP ALA ILE VAL HIS SER ILE          
SEQRES   8 B  268  ALA PHE ALA PRO ARG ASP GLN LEU GLU GLY ASN PHE ILE          
SEQRES   9 B  268  ASP CYS VAL THR ARG GLU GLY PHE SER ILE ALA HIS ASP          
SEQRES  10 B  268  ILE SER ALA TYR SER PHE ALA ALA LEU ALA LYS GLU GLY          
SEQRES  11 B  268  ARG SER MET MET LYS ASN ARG ASN ALA SER MET VAL ALA          
SEQRES  12 B  268  LEU THR TYR ILE GLY ALA GLU LYS ALA MET PRO SER TYR          
SEQRES  13 B  268  ASN THR MET GLY VAL ALA LYS ALA SER LEU GLU ALA THR          
SEQRES  14 B  268  VAL ARG TYR THR ALA LEU ALA LEU GLY GLU ASP GLY ILE          
SEQRES  15 B  268  LYS VAL ASN ALA VAL SER ALA GLY PRO ILE LYS THR LEU          
SEQRES  16 B  268  ALA ALA SER GLY ILE SER ASN PHE LYS LYS MET LEU ASP          
SEQRES  17 B  268  TYR ASN ALA MET VAL SER PRO LEU LYS LYS ASN VAL ASP          
SEQRES  18 B  268  ILE MET GLU VAL GLY ASN THR VAL ALA PHE LEU CYS SER          
SEQRES  19 B  268  ASP MET ALA THR GLY ILE THR GLY GLU VAL VAL HIS VAL          
SEQRES  20 B  268  ASP ALA GLY TYR HIS CYS VAL SER MET GLY ASN VAL LEU          
SEQRES  21 B  268  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  268  MET GLY PHE LEU ALA GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 C  268  LEU LEU SER ASN LYS SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 C  268  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 C  268  VAL GLY GLN PHE LYS ASP ARG VAL GLU LYS LEU CYS ALA          
SEQRES   5 C  268  GLU PHE ASN PRO ALA ALA VAL LEU PRO CYS ASP VAL ILE          
SEQRES   6 C  268  SER ASP GLN GLU ILE LYS ASP LEU PHE VAL GLU LEU GLY          
SEQRES   7 C  268  LYS VAL TRP ASP GLY LEU ASP ALA ILE VAL HIS SER ILE          
SEQRES   8 C  268  ALA PHE ALA PRO ARG ASP GLN LEU GLU GLY ASN PHE ILE          
SEQRES   9 C  268  ASP CYS VAL THR ARG GLU GLY PHE SER ILE ALA HIS ASP          
SEQRES  10 C  268  ILE SER ALA TYR SER PHE ALA ALA LEU ALA LYS GLU GLY          
SEQRES  11 C  268  ARG SER MET MET LYS ASN ARG ASN ALA SER MET VAL ALA          
SEQRES  12 C  268  LEU THR TYR ILE GLY ALA GLU LYS ALA MET PRO SER TYR          
SEQRES  13 C  268  ASN THR MET GLY VAL ALA LYS ALA SER LEU GLU ALA THR          
SEQRES  14 C  268  VAL ARG TYR THR ALA LEU ALA LEU GLY GLU ASP GLY ILE          
SEQRES  15 C  268  LYS VAL ASN ALA VAL SER ALA GLY PRO ILE LYS THR LEU          
SEQRES  16 C  268  ALA ALA SER GLY ILE SER ASN PHE LYS LYS MET LEU ASP          
SEQRES  17 C  268  TYR ASN ALA MET VAL SER PRO LEU LYS LYS ASN VAL ASP          
SEQRES  18 C  268  ILE MET GLU VAL GLY ASN THR VAL ALA PHE LEU CYS SER          
SEQRES  19 C  268  ASP MET ALA THR GLY ILE THR GLY GLU VAL VAL HIS VAL          
SEQRES  20 C  268  ASP ALA GLY TYR HIS CYS VAL SER MET GLY ASN VAL LEU          
SEQRES  21 C  268  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  268  MET GLY PHE LEU ALA GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 D  268  LEU LEU SER ASN LYS SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 D  268  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 D  268  VAL GLY GLN PHE LYS ASP ARG VAL GLU LYS LEU CYS ALA          
SEQRES   5 D  268  GLU PHE ASN PRO ALA ALA VAL LEU PRO CYS ASP VAL ILE          
SEQRES   6 D  268  SER ASP GLN GLU ILE LYS ASP LEU PHE VAL GLU LEU GLY          
SEQRES   7 D  268  LYS VAL TRP ASP GLY LEU ASP ALA ILE VAL HIS SER ILE          
SEQRES   8 D  268  ALA PHE ALA PRO ARG ASP GLN LEU GLU GLY ASN PHE ILE          
SEQRES   9 D  268  ASP CYS VAL THR ARG GLU GLY PHE SER ILE ALA HIS ASP          
SEQRES  10 D  268  ILE SER ALA TYR SER PHE ALA ALA LEU ALA LYS GLU GLY          
SEQRES  11 D  268  ARG SER MET MET LYS ASN ARG ASN ALA SER MET VAL ALA          
SEQRES  12 D  268  LEU THR TYR ILE GLY ALA GLU LYS ALA MET PRO SER TYR          
SEQRES  13 D  268  ASN THR MET GLY VAL ALA LYS ALA SER LEU GLU ALA THR          
SEQRES  14 D  268  VAL ARG TYR THR ALA LEU ALA LEU GLY GLU ASP GLY ILE          
SEQRES  15 D  268  LYS VAL ASN ALA VAL SER ALA GLY PRO ILE LYS THR LEU          
SEQRES  16 D  268  ALA ALA SER GLY ILE SER ASN PHE LYS LYS MET LEU ASP          
SEQRES  17 D  268  TYR ASN ALA MET VAL SER PRO LEU LYS LYS ASN VAL ASP          
SEQRES  18 D  268  ILE MET GLU VAL GLY ASN THR VAL ALA PHE LEU CYS SER          
SEQRES  19 D  268  ASP MET ALA THR GLY ILE THR GLY GLU VAL VAL HIS VAL          
SEQRES  20 D  268  ASP ALA GLY TYR HIS CYS VAL SER MET GLY ASN VAL LEU          
SEQRES  21 D  268  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET    NAD  D1261      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   5  NAD    C21 H27 N7 O14 P2                                            
HELIX    1   1 SER A   19  GLU A   31  1                                  13    
HELIX    2   2 PHE A   43  ALA A   52  1                                  10    
HELIX    3   3 GLU A   53  ASN A   55  5                                   3    
HELIX    4   4 SER A   66  TRP A   81  1                                  16    
HELIX    5   5 PRO A   95  LEU A   99  5                                   5    
HELIX    6   6 ASN A  102  VAL A  107  1                                   6    
HELIX    7   7 THR A  108  ALA A  120  1                                  13    
HELIX    8   8 ALA A  120  ARG A  131  1                                  12    
HELIX    9   9 SER A  132  LYS A  135  5                                   4    
HELIX   10  10 TYR A  146  GLU A  150  5                                   5    
HELIX   11  11 TYR A  156  LEU A  177  1                                  22    
HELIX   12  12 MET A  206  SER A  214  1                                   9    
HELIX   13  13 ASP A  221  LEU A  232  1                                  12    
HELIX   14  14 CYS A  233  THR A  238  5                                   6    
HELIX   15  15 GLY A  250  CYS A  253  5                                   4    
HELIX   16  16 SER B   19  GLU B   31  1                                  13    
HELIX   17  17 VAL B   40  GLN B   42  5                                   3    
HELIX   18  18 PHE B   43  ALA B   52  1                                  10    
HELIX   19  19 GLU B   53  ASN B   55  5                                   3    
HELIX   20  20 SER B   66  TRP B   81  1                                  16    
HELIX   21  21 PRO B   95  LEU B   99  5                                   5    
HELIX   22  22 ASN B  102  VAL B  107  1                                   6    
HELIX   23  23 THR B  108  ALA B  120  1                                  13    
HELIX   24  24 ALA B  120  ARG B  131  1                                  12    
HELIX   25  25 SER B  132  MET B  134  5                                   3    
HELIX   26  26 TYR B  146  GLU B  150  5                                   5    
HELIX   27  27 TYR B  156  GLY B  178  1                                  23    
HELIX   28  28 GLU B  179  GLY B  181  5                                   3    
HELIX   29  29 ASP B  221  LEU B  232  1                                  12    
HELIX   30  30 CYS B  233  THR B  238  5                                   6    
HELIX   31  31 GLY B  250  CYS B  253  5                                   4    
HELIX   32  32 SER C   19  GLU C   31  1                                  13    
HELIX   33  33 PHE C   43  ALA C   52  1                                  10    
HELIX   34  34 GLU C   53  ASN C   55  5                                   3    
HELIX   35  35 SER C   66  TRP C   81  1                                  16    
HELIX   36  36 PRO C   95  LEU C   99  5                                   5    
HELIX   37  37 ASN C  102  VAL C  107  1                                   6    
HELIX   38  38 THR C  108  ALA C  120  1                                  13    
HELIX   39  39 ALA C  120  LYS C  135  1                                  16    
HELIX   40  40 TYR C  146  GLU C  150  5                                   5    
HELIX   41  41 TYR C  156  GLY C  178  1                                  23    
HELIX   42  42 GLU C  179  GLY C  181  5                                   3    
HELIX   43  43 TYR C  209  SER C  214  1                                   6    
HELIX   44  44 ASP C  221  LEU C  232  1                                  12    
HELIX   45  45 CYS C  233  THR C  238  5                                   6    
HELIX   46  46 GLY C  250  CYS C  253  5                                   4    
HELIX   47  47 SER D   19  GLU D   31  1                                  13    
HELIX   48  48 PHE D   43  ALA D   52  1                                  10    
HELIX   49  49 GLU D   53  ASN D   55  5                                   3    
HELIX   50  50 SER D   66  GLY D   78  1                                  13    
HELIX   51  51 PRO D   95  LEU D   99  5                                   5    
HELIX   52  52 ASN D  102  VAL D  107  1                                   6    
HELIX   53  53 THR D  108  ALA D  120  1                                  13    
HELIX   54  54 ALA D  120  ARG D  131  1                                  12    
HELIX   55  55 SER D  132  MET D  134  5                                   3    
HELIX   56  56 ASN D  157  LEU D  177  1                                  21    
HELIX   57  57 MET D  206  SER D  214  1                                   9    
HELIX   58  58 ASP D  221  LEU D  232  1                                  12    
HELIX   59  59 CYS D  233  THR D  238  5                                   6    
HELIX   60  60 GLY D  250  CYS D  253  5                                   4    
SHEET    1  AA 7 ALA A  58  PRO A  61  0                                        
SHEET    2  AA 7 GLU A  34  TYR A  39  1  O  PHE A  37   N  LEU A  60           
SHEET    3  AA 7 LYS A   8  ILE A  11  1  O  ILE A   9   N  ALA A  36           
SHEET    4  AA 7 ALA A  86  HIS A  89  1  O  ALA A  86   N  LEU A  10           
SHEET    5  AA 7 SER A 140  THR A 145  1  O  SER A 140   N  ILE A  87           
SHEET    6  AA 7 LYS A 183  ALA A 189  1  O  LYS A 183   N  MET A 141           
SHEET    7  AA 7 VAL A 244  VAL A 247  1  O  VAL A 245   N  SER A 188           
SHEET    1  AB 2 LEU A 260  LEU A 261  0                                        
SHEET    2  AB 2 LEU C 260  LEU C 261  1  O  LEU C 260   N  LEU A 261           
SHEET    1  AC 2 HIS A 264  HIS A 267  0                                        
SHEET    2  AC 2 HIS C 264  HIS C 267  1  O  HIS C 264   N  HIS A 265           
SHEET    1  BA 7 ALA B  58  PRO B  61  0                                        
SHEET    2  BA 7 GLU B  34  TYR B  39  1  O  PHE B  37   N  LEU B  60           
SHEET    3  BA 7 LYS B   8  ILE B  11  1  O  ILE B   9   N  ALA B  36           
SHEET    4  BA 7 ALA B  86  HIS B  89  1  O  ALA B  86   N  LEU B  10           
SHEET    5  BA 7 SER B 140  THR B 145  1  O  SER B 140   N  ILE B  87           
SHEET    6  BA 7 LYS B 183  ALA B 189  1  O  LYS B 183   N  MET B 141           
SHEET    7  BA 7 VAL B 244  VAL B 247  1  O  VAL B 245   N  SER B 188           
SHEET    1  CA 7 ALA C  58  PRO C  61  0                                        
SHEET    2  CA 7 GLU C  34  TYR C  39  1  O  PHE C  37   N  LEU C  60           
SHEET    3  CA 7 LYS C   8  ILE C  11  1  O  ILE C   9   N  ALA C  36           
SHEET    4  CA 7 ALA C  86  HIS C  89  1  O  ALA C  86   N  LEU C  10           
SHEET    5  CA 7 SER C 140  THR C 145  1  O  SER C 140   N  ILE C  87           
SHEET    6  CA 7 LYS C 183  ALA C 189  1  O  LYS C 183   N  MET C 141           
SHEET    7  CA 7 VAL C 244  VAL C 247  1  O  VAL C 245   N  SER C 188           
SHEET    1  DA 7 ALA D  58  PRO D  61  0                                        
SHEET    2  DA 7 GLU D  34  TYR D  39  1  O  PHE D  37   N  LEU D  60           
SHEET    3  DA 7 LYS D   8  ILE D  11  1  O  ILE D   9   N  ALA D  36           
SHEET    4  DA 7 ALA D  86  HIS D  89  1  O  ALA D  86   N  LEU D  10           
SHEET    5  DA 7 SER D 140  TYR D 146  1  O  SER D 140   N  ILE D  87           
SHEET    6  DA 7 LYS D 183  ALA D 189  1  O  LYS D 183   N  MET D 141           
SHEET    7  DA 7 VAL D 244  VAL D 247  1  O  VAL D 245   N  SER D 188           
SITE     1 AC1 18 GLY D  13  LEU D  15  SER D  19  ILE D  20                    
SITE     2 AC1 18 VAL D  40  CYS D  62  ASP D  63  VAL D  64                    
SITE     3 AC1 18 SER D  90  ILE D  91  ALA D  92  ILE D 118                    
SITE     4 AC1 18 LEU D 144  TYR D 146  LYS D 163  GLY D 190                    
SITE     5 AC1 18 PRO D 191  ILE D 192                                          
CRYST1   96.006   99.454  111.032  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010416  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010055  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009006        0.00000                         
MTRIX1   1 -0.362400  0.715500 -0.597300      -15.96000    1                    
MTRIX2   1  0.723100 -0.188500 -0.664500       16.30000    1                    
MTRIX3   1 -0.588000 -0.672800 -0.449100        2.61000    1                    
MTRIX1   2 -0.755700  0.271500  0.595900      -39.14000    1                    
MTRIX2   2  0.275500 -0.693800  0.665400       -9.74000    1                    
MTRIX3   2  0.594100  0.667100  0.449500       20.67000    1                    
MTRIX1   3  0.131200 -0.991300  0.005114      -20.98000    1                    
MTRIX2   3 -0.991400 -0.131200 -0.000349      -23.96000    1                    
MTRIX3   3  0.001017 -0.005024 -1.000000       22.93000    1                    
MTRIX1   4 -0.364000  0.711800 -0.600700      -15.91000    1                    
MTRIX2   4  0.723300 -0.190300 -0.663800       16.25000    1                    
MTRIX3   4 -0.586800 -0.676100 -0.445600        2.58400    1                    
MTRIX1   5 -0.753400  0.273800  0.597800      -39.02000    1                    
MTRIX2   5  0.276200 -0.693300  0.665600       -9.81000    1                    
MTRIX3   5  0.596700  0.666600  0.446700       20.78000    1                    
MTRIX1   6  0.122600 -0.992500 -0.001494      -21.01000    1                    
MTRIX2   6 -0.992500 -0.122600 -0.002326      -23.84000    1                    
MTRIX3   6  0.002125  0.001768 -1.000000       23.09000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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