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Database: PDB
Entry: 4JX8
LinkDB: 4JX8
Original site: 4JX8 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 28-MAR-13   4JX8              
TITLE     CRYSTAL STRUCTURE OF E.COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND   
TITLE    2 AEA16                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ENR, NADH-DEPENDENT ENOYL-ACP REDUCTASE;                    
COMPND   5 EC: 1.3.1.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: FABI, ENVM, B1288, JW1281;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    FABI, LIGAND AEA16, ENOYL REDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SUBRAMANYA,K.N.RAO,L.ANIRUDHA                                       
REVDAT   1   02-APR-14 4JX8    0                                                
JRNL        AUTH   H.SUBRAMANYA,K.N.RAO,L.ANIRUDHA                              
JRNL        TITL   CRYSTAL STRUCTURE OF E.COLI ENOYL REDUCTASE IN COMPLEX WITH  
JRNL        TITL 2 NAD AND AEA16                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 7942                           
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.326                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 403                             
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 454                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 22                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3696                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 146                                     
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.819         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.477         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.243        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.879                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.702                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3914 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5317 ; 1.911 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   497 ; 6.460 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;38.778 ;24.156       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   596 ;18.350 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;15.015 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   602 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2944 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4JX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078618.                                      
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                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FLITER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8204                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
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: 1QSG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.6, 10%-15%      
REMARK 280  (W/V) PEG 4000, 200MM AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING    
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.78400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      215.56800            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      161.67600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      269.46000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.89200            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      107.78400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      215.56800            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      269.46000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      161.67600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       53.89200            
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: 5660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     LEU A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B   193                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     ILE B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     PHE B   203                                                      
REMARK 465     ARG B   204                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     MET B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     ALA B   208                                                      
REMARK 465     LEU B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
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     MET A   1    CG   SD   CE                                        
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     LEU A  18    CG   CD1  CD2                                       
REMARK 470     SER A  19    OG                                                  
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     HIS B 209    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A   180     O    HOH A   417              1.70            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN B    41     O    HOH A   406     8567     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   4   CB  -  CA  -  C   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ASP A 101   N   -  CA  -  C   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    GLY A 102   N   -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ASN A 155   CB  -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    TYR A 156   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    MET A 159   CB  -  CA  -  C   ANGL. DEV. =  15.5 DEGREES          
REMARK 500    LEU A 161   N   -  CA  -  C   ANGL. DEV. = -21.7 DEGREES          
REMARK 500    GLU A 180   CB  -  CA  -  C   ANGL. DEV. = -21.1 DEGREES          
REMARK 500    ARG A 193   CB  -  CA  -  C   ANGL. DEV. = -29.7 DEGREES          
REMARK 500    ARG A 193   N   -  CA  -  C   ANGL. DEV. =  28.0 DEGREES          
REMARK 500    CYS A 210   C   -  N   -  CA  ANGL. DEV. = -30.2 DEGREES          
REMARK 500    ALA A 238   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    LEU B 100   N   -  CA  -  CB  ANGL. DEV. = -20.8 DEGREES          
REMARK 500    LEU B 195   CB  -  CA  -  C   ANGL. DEV. =  21.4 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    ILE A  20      -55.52     67.65                                   
REMARK 500    ARG A  47      -72.87    130.44                                   
REMARK 500    CYS A  63       97.58   -164.10                                   
REMARK 500    VAL A  65        4.34    -66.05                                   
REMARK 500    SER A  91       41.26   -109.82                                   
REMARK 500    PRO A  96      133.56    -38.57                                   
REMARK 500    ASP A  98      -32.19    -33.52                                   
REMARK 500    LEU A 100       44.68   -100.86                                   
REMARK 500    ASP A 101      -70.65    -80.53                                   
REMARK 500    ASP A 103      130.28    -39.12                                   
REMARK 500    SER A 121      -58.28   -129.72                                   
REMARK 500    ASN A 155       18.91     49.25                                   
REMARK 500    ASN A 157     -125.28     44.56                                   
REMARK 500    PRO A 179      -56.29    -28.33                                   
REMARK 500    ILE A 192       33.00     75.10                                   
REMARK 500    THR A 194     -149.15   -120.01                                   
REMARK 500    ALA A 197        8.67    -63.96                                   
REMARK 500    HIS A 209       34.33     77.78                                   
REMARK 500    ALA A 238      -34.19    -35.01                                   
REMARK 500    VAL A 247       64.22   -114.37                                   
REMARK 500    ALA B  15      -12.95   -144.12                                   
REMARK 500    ASP B  58       58.76   -150.93                                   
REMARK 500    HIS B  90       72.35   -108.80                                   
REMARK 500    SER B  91       55.02    -92.51                                   
REMARK 500    ASP B  98      -59.20     69.36                                   
REMARK 500    LEU B 100       54.14   -113.04                                   
REMARK 500    SER B 121      -56.22   -140.53                                   
REMARK 500    ASN B 155       -3.81     76.89                                   
REMARK 500    ASN B 157     -119.80     52.57                                   
REMARK 500    LEU B 195     -166.88   -168.66                                   
REMARK 500    SER B 237       41.79    -90.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  160     LEU A  161                  149.96                    
REMARK 500 GLU A  180     GLY A  181                  147.87                    
REMARK 500 PRO A  191     ILE A  192                   32.76                    
REMARK 500 ALA A  208     HIS A  209                 -149.26                    
REMARK 500 HIS A  209     CYS A  210                   84.37                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A 208        -12.33                                           
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    ASP A 101        23.0      L          L   OUTSIDE RANGE           
REMARK 500    MET A 159        16.0      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 192        19.3      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 193        21.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 100        50.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 195        24.7      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 AE6 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE6 B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JQC   RELATED DB: PDB                                   
DBREF  4JX8 A    1   262  UNP    P0AEK4   FABI_ECOLI       1    262             
DBREF  4JX8 B    1   262  UNP    P0AEK4   FABI_ECOLI       1    262             
SEQADV 4JX8 MET A  -19  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY A  -18  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER A  -17  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER A  -16  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -15  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -14  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -13  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -12  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -11  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A  -10  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER A   -9  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER A   -8  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY A   -7  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 LEU A   -6  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 VAL A   -5  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 PRO A   -4  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 ARG A   -3  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY A   -2  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER A   -1  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS A    0  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 MET B  -19  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY B  -18  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER B  -17  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER B  -16  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -15  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -14  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -13  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -12  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -11  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B  -10  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER B   -9  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER B   -8  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY B   -7  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 LEU B   -6  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 VAL B   -5  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 PRO B   -4  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 ARG B   -3  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 GLY B   -2  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 SER B   -1  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 4JX8 HIS B    0  UNP  P0AEK4              EXPRESSION TAG                 
SEQRES   1 A  282  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  282  LEU VAL PRO ARG GLY SER HIS MET GLY PHE LEU SER GLY          
SEQRES   3 A  282  LYS ARG ILE LEU VAL THR GLY VAL ALA SER LYS LEU SER          
SEQRES   4 A  282  ILE ALA TYR GLY ILE ALA GLN ALA MET HIS ARG GLU GLY          
SEQRES   5 A  282  ALA GLU LEU ALA PHE THR TYR GLN ASN ASP LYS LEU LYS          
SEQRES   6 A  282  GLY ARG VAL GLU GLU PHE ALA ALA GLN LEU GLY SER ASP          
SEQRES   7 A  282  ILE VAL LEU GLN CYS ASP VAL ALA GLU ASP ALA SER ILE          
SEQRES   8 A  282  ASP THR MET PHE ALA GLU LEU GLY LYS VAL TRP PRO LYS          
SEQRES   9 A  282  PHE ASP GLY PHE VAL HIS SER ILE GLY PHE ALA PRO GLY          
SEQRES  10 A  282  ASP GLN LEU ASP GLY ASP TYR VAL ASN ALA VAL THR ARG          
SEQRES  11 A  282  GLU GLY PHE LYS ILE ALA HIS ASP ILE SER SER TYR SER          
SEQRES  12 A  282  PHE VAL ALA MET ALA LYS ALA CYS ARG SER MET LEU ASN          
SEQRES  13 A  282  PRO GLY SER ALA LEU LEU THR LEU SER TYR LEU GLY ALA          
SEQRES  14 A  282  GLU ARG ALA ILE PRO ASN TYR ASN VAL MET GLY LEU ALA          
SEQRES  15 A  282  LYS ALA SER LEU GLU ALA ASN VAL ARG TYR MET ALA ASN          
SEQRES  16 A  282  ALA MET GLY PRO GLU GLY VAL ARG VAL ASN ALA ILE SER          
SEQRES  17 A  282  ALA GLY PRO ILE ARG THR LEU ALA ALA SER GLY ILE LYS          
SEQRES  18 A  282  ASP PHE ARG LYS MET LEU ALA HIS CYS GLU ALA VAL THR          
SEQRES  19 A  282  PRO ILE ARG ARG THR VAL THR ILE GLU ASP VAL GLY ASN          
SEQRES  20 A  282  SER ALA ALA PHE LEU CYS SER ASP LEU SER ALA GLY ILE          
SEQRES  21 A  282  SER GLY GLU VAL VAL HIS VAL ASP GLY GLY PHE SER ILE          
SEQRES  22 A  282  ALA ALA MET ASN GLU LEU GLU LEU LYS                          
SEQRES   1 B  282  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  282  LEU VAL PRO ARG GLY SER HIS MET GLY PHE LEU SER GLY          
SEQRES   3 B  282  LYS ARG ILE LEU VAL THR GLY VAL ALA SER LYS LEU SER          
SEQRES   4 B  282  ILE ALA TYR GLY ILE ALA GLN ALA MET HIS ARG GLU GLY          
SEQRES   5 B  282  ALA GLU LEU ALA PHE THR TYR GLN ASN ASP LYS LEU LYS          
SEQRES   6 B  282  GLY ARG VAL GLU GLU PHE ALA ALA GLN LEU GLY SER ASP          
SEQRES   7 B  282  ILE VAL LEU GLN CYS ASP VAL ALA GLU ASP ALA SER ILE          
SEQRES   8 B  282  ASP THR MET PHE ALA GLU LEU GLY LYS VAL TRP PRO LYS          
SEQRES   9 B  282  PHE ASP GLY PHE VAL HIS SER ILE GLY PHE ALA PRO GLY          
SEQRES  10 B  282  ASP GLN LEU ASP GLY ASP TYR VAL ASN ALA VAL THR ARG          
SEQRES  11 B  282  GLU GLY PHE LYS ILE ALA HIS ASP ILE SER SER TYR SER          
SEQRES  12 B  282  PHE VAL ALA MET ALA LYS ALA CYS ARG SER MET LEU ASN          
SEQRES  13 B  282  PRO GLY SER ALA LEU LEU THR LEU SER TYR LEU GLY ALA          
SEQRES  14 B  282  GLU ARG ALA ILE PRO ASN TYR ASN VAL MET GLY LEU ALA          
SEQRES  15 B  282  LYS ALA SER LEU GLU ALA ASN VAL ARG TYR MET ALA ASN          
SEQRES  16 B  282  ALA MET GLY PRO GLU GLY VAL ARG VAL ASN ALA ILE SER          
SEQRES  17 B  282  ALA GLY PRO ILE ARG THR LEU ALA ALA SER GLY ILE LYS          
SEQRES  18 B  282  ASP PHE ARG LYS MET LEU ALA HIS CYS GLU ALA VAL THR          
SEQRES  19 B  282  PRO ILE ARG ARG THR VAL THR ILE GLU ASP VAL GLY ASN          
SEQRES  20 B  282  SER ALA ALA PHE LEU CYS SER ASP LEU SER ALA GLY ILE          
SEQRES  21 B  282  SER GLY GLU VAL VAL HIS VAL ASP GLY GLY PHE SER ILE          
SEQRES  22 B  282  ALA ALA MET ASN GLU LEU GLU LEU LYS                          
HET    AE6  A 301      29                                                       
HET    NAD  A 302      44                                                       
HET    NAD  B 301      44                                                       
HET    AE6  B 302      29                                                       
HETNAM     AE6 6-{(1E)-3-[3-(3-METHYL-1-BENZOFURAN-2-YL)AZETIDIN-1-             
HETNAM   2 AE6  YL]-3-OXOPROP-1-EN-1-YL}-1,8-NAPHTHYRIDIN-2(1H)-ONE             
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  AE6    2(C23 H19 N3 O3)                                             
FORMUL   4  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   7  HOH   *54(H2 O)                                                     
HELIX    1   1 ILE A   20  GLU A   31  1                                  12    
HELIX    2   2 ASN A   41  LEU A   55  1                                  15    
HELIX    3   3 GLU A   67  LYS A   80  1                                  14    
HELIX    4   4 PRO A   96  ASP A  101  5                                   6    
HELIX    5   5 ASP A  103  VAL A  108  1                                   6    
HELIX    6   6 THR A  109  SER A  121  1                                  13    
HELIX    7   7 SER A  121  ARG A  132  1                                  12    
HELIX    8   8 SER A  133  LEU A  135  5                                   3    
HELIX    9   9 TYR A  146  GLU A  150  5                                   5    
HELIX   10  10 TYR A  156  LEU A  161  5                                   6    
HELIX   11  11 ALA A  162  GLY A  178  1                                  17    
HELIX   12  12 THR A  194  GLY A  199  5                                   6    
HELIX   13  13 ASP A  202  LEU A  207  1                                   6    
HELIX   14  14 THR A  221  CYS A  233  1                                  13    
HELIX   15  15 SER A  234  ALA A  238  5                                   5    
HELIX   16  16 GLY A  250  ALA A  254  5                                   5    
HELIX   17  17 SER B   19  GLU B   31  1                                  13    
HELIX   18  18 ASN B   41  LEU B   55  1                                  15    
HELIX   19  19 GLU B   67  TRP B   82  1                                  16    
HELIX   20  20 ASP B  103  VAL B  108  1                                   6    
HELIX   21  21 THR B  109  SER B  121  1                                  13    
HELIX   22  22 SER B  121  ARG B  132  1                                  12    
HELIX   23  23 SER B  133  LEU B  135  5                                   3    
HELIX   24  24 ASN B  157  GLY B  178  1                                  22    
HELIX   25  25 THR B  221  SER B  234  1                                  14    
HELIX   26  26 ASP B  235  ALA B  238  5                                   4    
SHEET    1   A 7 VAL A  60  GLN A  62  0                                        
SHEET    2   A 7 GLU A  34  TYR A  39  1  N  PHE A  37   O  LEU A  61           
SHEET    3   A 7 ARG A   8  VAL A  11  1  N  VAL A  11   O  ALA A  36           
SHEET    4   A 7 PHE A  88  HIS A  90  1  O  VAL A  89   N  LEU A  10           
SHEET    5   A 7 SER A 139  SER A 145  1  O  LEU A 142   N  HIS A  90           
SHEET    6   A 7 VAL A 182  ALA A 189  1  O  ARG A 183   N  LEU A 141           
SHEET    7   A 7 VAL A 244  VAL A 247  1  O  VAL A 245   N  SER A 188           
SHEET    1   B 7 VAL B  60  GLN B  62  0                                        
SHEET    2   B 7 GLU B  34  TYR B  39  1  N  PHE B  37   O  LEU B  61           
SHEET    3   B 7 ARG B   8  VAL B  11  1  N  VAL B  11   O  ALA B  36           
SHEET    4   B 7 PHE B  88  HIS B  90  1  O  VAL B  89   N  LEU B  10           
SHEET    5   B 7 SER B 139  SER B 145  1  O  LEU B 142   N  PHE B  88           
SHEET    6   B 7 VAL B 182  ALA B 189  1  O  ARG B 183   N  LEU B 141           
SHEET    7   B 7 GLU B 243  VAL B 247  1  O  VAL B 245   N  SER B 188           
CISPEP   1 GLY A   46    ARG A   47          0         7.02                     
CISPEP   2 ASN A  257    GLU A  258          0       -14.82                     
CISPEP   3 GLY B   97    ASP B   98          0        -1.68                     
SITE     1 AC1 14 PHE A  94  ALA A  95  GLY A  97  TYR A 146                    
SITE     2 AC1 14 ILE A 153  PRO A 154  TYR A 156  MET A 159                    
SITE     3 AC1 14 PRO A 191  ALA A 196  GLY A 199  ILE A 200                    
SITE     4 AC1 14 MET A 206  NAD A 302                                          
SITE     1 AC2 23 GLY A  13  VAL A  14  ALA A  15  SER A  19                    
SITE     2 AC2 23 ILE A  20  GLN A  40  CYS A  63  ASP A  64                    
SITE     3 AC2 23 VAL A  65  SER A  91  ILE A  92  GLY A  93                    
SITE     4 AC2 23 LEU A 144  SER A 145  TYR A 146  LYS A 163                    
SITE     5 AC2 23 ALA A 189  PRO A 191  ILE A 192  THR A 194                    
SITE     6 AC2 23 LEU A 195  ALA A 196  AE6 A 301                               
SITE     1 AC3 18 GLY B  13  ALA B  15  ILE B  20  GLN B  40                    
SITE     2 AC3 18 CYS B  63  ASP B  64  VAL B  65  SER B  91                    
SITE     3 AC3 18 ILE B  92  GLY B  93  LEU B 144  SER B 145                    
SITE     4 AC3 18 LYS B 163  ALA B 189  GLY B 190  THR B 194                    
SITE     5 AC3 18 LEU B 195  AE6 B 302                                          
SITE     1 AC4  8 GLY B  93  PHE B  94  ALA B  95  LEU B 100                    
SITE     2 AC4  8 ILE B 153  TYR B 156  ALA B 196  NAD B 301                    
CRYST1   79.632   79.632  323.352  90.00  90.00 120.00 P 61 2 2     24          
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      0.012558  0.007250  0.000000        0.00000                         
SCALE2      0.000000  0.014500  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003093        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system