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Database: PDB
Entry: 2F3X
LinkDB: 2F3X
Original site: 2F3X 
HEADER    GENE REGULATION                         22-NOV-05   2F3X              
TITLE     CRYSTAL STRUCTURE OF FAPR (IN COMPLEX WITH EFFECTOR)- A               
TITLE    2 GLOBAL REGULATOR OF FATTY ACID BIOSYNTHESIS IN B. SUBTILIS           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR FAPR;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TEMINAL DOMAIN + LINKER ALPHA HELIX (RESIDUES            
COMPND   5 44-188);                                                             
COMPND   6 SYNONYM: FATTY ACID AND PHOSPHOLIPID BIOSYNTHESIS                    
COMPND   7 REGULATOR;                                                           
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: FAPR;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    'HOT-DOG' FOLD / MALONYL-COA COMPLEX, GENE REGULATION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BUSCHIAZZO,M.E.GUERIN,P.M.ALZARI                                    
REVDAT   2   24-FEB-09 2F3X    1       VERSN                                    
REVDAT   1   31-OCT-06 2F3X    0                                                
JRNL        AUTH   G.E.SCHUJMAN,M.GUERIN,A.BUSCHIAZZO,F.SCHAEFFER,              
JRNL        AUTH 2 L.I.LLARRULL,G.REH,A.J.VILA,P.M.ALZARI,D.DE MENDOZA          
JRNL        TITL   STRUCTURAL BASIS OF LIPID BIOSYNTHESIS REGULATION            
JRNL        TITL 2 IN GRAM-POSITIVE BACTERIA.                                   
JRNL        REF    EMBO J.                       V.  25  4074 2006              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   16932747                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7601284                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 12545                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 941                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 841                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2238                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.69000                                              
REMARK   3    B22 (A**2) : 0.69000                                              
REMARK   3    B33 (A**2) : -1.39000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.591         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.321         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.215         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.708        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2320 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2177 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3132 ; 2.137 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5045 ; 0.945 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   284 ; 8.360 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;35.850 ;24.821       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   425 ;22.542 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.749 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   366 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2551 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   436 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   471 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2374 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1131 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1629 ; 0.098 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    58 ; 0.146 ; 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):    15 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    32 ; 0.218 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.102 ; 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):  1460 ; 0.793 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   586 ; 0.117 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2286 ; 1.275 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   937 ; 1.934 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   846 ; 3.342 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2F3X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035421.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : KHOZU MONOCHROMATOR WITH A         
REMARK 200                                   MCLENNON CONTROLLER CONTAINING     
REMARK 200                                   A LN2 COOLED SI111 CRYSTAL         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12596                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENGLYCOL, 5MM MALONYL-COA,      
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.08300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       44.72050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       44.72050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.54150            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       44.72050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       44.72050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.62450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       44.72050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.72050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.54150            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       44.72050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.72050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      121.62450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       81.08300            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY CORRESPONDS TO THE DIMER IN THE      
REMARK 300 ASU                                                                  
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: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     HIS A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     HIS A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     HIS A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     MET B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     HIS B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     HIS B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     HIS B   187                                                      
REMARK 465     SER B   188                                                      
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     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 151    CG   CD   CE   NZ                                   
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     GLU A 158    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  77   CG    GLU A  77   CD      0.116                       
REMARK 500    GLU A 172   CB    GLU A 172   CG      0.122                       
REMARK 500    GLU A 172   CG    GLU A 172   CD      0.104                       
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    VAL A 121   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL B 121   CB  -  CA  -  C   ANGL. DEV. = -12.9 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    LEU A  45      155.42     85.34                                   
REMARK 500    ASP A  85      -79.81   -150.18                                   
REMARK 500    ASN A 102       19.00   -152.16                                   
REMARK 500    LYS A 159       41.13     35.12                                   
REMARK 500    ARG A 184      -88.59   -141.46                                   
REMARK 500    SER A 185       74.13    159.55                                   
REMARK 500    ASP B  72      -49.88    -20.76                                   
REMARK 500    ASP B  84       25.42     25.78                                   
REMARK 500    ASP B  85      -76.05   -136.23                                   
REMARK 500    ASP B 124      148.92    177.10                                   
REMARK 500    ALA B 154      121.16   -179.23                                   
REMARK 500    GLU B 156       60.08   -162.11                                   
REMARK 500    GLU B 158      -88.68    -40.32                                   
REMARK 500    LYS B 159       34.16    -73.55                                   
REMARK 500    SER B 185      147.87    139.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  10        DISTANCE = 25.26 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 NUCLEOTIDIC PORTION OF MLC COULD NOT BE MODELED                      
REMARK 600 DUE TO LACK OF ELECTRON DENSITY.                                     
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MLC B  390                                                       
REMARK 610     MLC A  391                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLC B 390                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLC A 391                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F41   RELATED DB: PDB                                   
DBREF  2F3X A   44   188  UNP    O34835   FAPR_BACSU      44    188             
DBREF  2F3X B   44   188  UNP    O34835   FAPR_BACSU      44    188             
SEQADV 2F3X MET A   32  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X ARG A   33  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X GLY A   34  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X SER A   35  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X HIS A   36  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS A   37  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS A   38  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS A   39  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS A   40  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS A   41  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X GLY A   42  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X SER A   43  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X MET B   32  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X ARG B   33  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X GLY B   34  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X SER B   35  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X HIS B   36  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS B   37  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS B   38  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS B   39  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS B   40  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X HIS B   41  UNP  O34835              EXPRESSION TAG                 
SEQADV 2F3X GLY B   42  UNP  O34835              CLONING ARTIFACT               
SEQADV 2F3X SER B   43  UNP  O34835              CLONING ARTIFACT               
SEQRES   1 A  157  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU          
SEQRES   2 A  157  LEU SER ILE PRO GLU LEU ARG GLU ARG ILE LYS ASN VAL          
SEQRES   3 A  157  ALA GLU LYS THR LEU GLU ASP GLU VAL LYS SER LEU SER          
SEQRES   4 A  157  LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP LEU GLU LEU          
SEQRES   5 A  157  ASP ASP GLN ALA ILE SER ILE LEU GLU ILE LYS GLN GLU          
SEQRES   6 A  157  HIS VAL PHE SER ARG ASN GLN ILE ALA ARG GLY HIS HIS          
SEQRES   7 A  157  LEU PHE ALA GLN ALA ASN SER LEU ALA VAL ALA VAL ILE          
SEQRES   8 A  157  ASP ASP GLU LEU ALA LEU THR ALA SER ALA ASP ILE ARG          
SEQRES   9 A  157  PHE THR ARG GLN VAL LYS GLN GLY GLU ARG VAL VAL ALA          
SEQRES  10 A  157  LYS ALA LYS VAL THR ALA VAL GLU LYS GLU LYS GLY ARG          
SEQRES  11 A  157  THR VAL VAL GLU VAL ASN SER TYR VAL GLY GLU GLU ILE          
SEQRES  12 A  157  VAL PHE SER GLY ARG PHE ASP MET TYR ARG SER LYS HIS          
SEQRES  13 A  157  SER                                                          
SEQRES   1 B  157  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU          
SEQRES   2 B  157  LEU SER ILE PRO GLU LEU ARG GLU ARG ILE LYS ASN VAL          
SEQRES   3 B  157  ALA GLU LYS THR LEU GLU ASP GLU VAL LYS SER LEU SER          
SEQRES   4 B  157  LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP LEU GLU LEU          
SEQRES   5 B  157  ASP ASP GLN ALA ILE SER ILE LEU GLU ILE LYS GLN GLU          
SEQRES   6 B  157  HIS VAL PHE SER ARG ASN GLN ILE ALA ARG GLY HIS HIS          
SEQRES   7 B  157  LEU PHE ALA GLN ALA ASN SER LEU ALA VAL ALA VAL ILE          
SEQRES   8 B  157  ASP ASP GLU LEU ALA LEU THR ALA SER ALA ASP ILE ARG          
SEQRES   9 B  157  PHE THR ARG GLN VAL LYS GLN GLY GLU ARG VAL VAL ALA          
SEQRES  10 B  157  LYS ALA LYS VAL THR ALA VAL GLU LYS GLU LYS GLY ARG          
SEQRES  11 B  157  THR VAL VAL GLU VAL ASN SER TYR VAL GLY GLU GLU ILE          
SEQRES  12 B  157  VAL PHE SER GLY ARG PHE ASP MET TYR ARG SER LYS HIS          
SEQRES  13 B  157  SER                                                          
HET    MLC  B 390      32                                                       
HET    MLC  A 391      32                                                       
HETNAM     MLC MALONYL-COENZYME A                                               
FORMUL   3  MLC    2(C24 H38 N7 O19 P3 S)                                       
FORMUL   5  HOH   *10(H2 O)                                                     
HELIX    1   1 SER A   46  ASP A   64  1                                  19    
HELIX    2   2 SER A   70  VAL A   74  5                                   5    
HELIX    3   3 LYS A   94  VAL A   98  5                                   5    
HELIX    4   4 ARG A  106  VAL A  121  1                                  16    
HELIX    5   5 LYS A  157  GLY A  160  5                                   4    
HELIX    6   6 SER B   46  LEU B   62  1                                  17    
HELIX    7   7 SER B   70  VAL B   74  5                                   5    
HELIX    8   8 LYS B   94  VAL B   98  5                                   5    
HELIX    9   9 ARG B  106  VAL B  121  1                                  16    
SHEET    1   A12 GLU A  77  GLU A  82  0                                        
SHEET    2   A12 GLN A  86  GLU A  92 -1  O  GLN A  86   N  GLU A  82           
SHEET    3   A12 ARG A 145  GLU A 156 -1  O  ALA A 150   N  ALA A  87           
SHEET    4   A12 ARG A 161  VAL A 170 -1  O  VAL A 163   N  ALA A 154           
SHEET    5   A12 GLU A 173  TYR A 183 -1  O  VAL A 175   N  SER A 168           
SHEET    6   A12 LEU A 128  PHE A 136 -1  N  LEU A 128   O  TYR A 183           
SHEET    7   A12 ALA B 127  PHE B 136 -1  O  PHE B 136   N  ALA A 130           
SHEET    8   A12 GLU B 173  ARG B 184 -1  O  ASP B 181   N  ALA B 130           
SHEET    9   A12 ARG B 161  VAL B 170 -1  N  SER B 168   O  PHE B 176           
SHEET   10   A12 ARG B 145  GLU B 156 -1  N  ALA B 154   O  VAL B 163           
SHEET   11   A12 GLN B  86  GLU B  92 -1  N  LEU B  91   O  VAL B 146           
SHEET   12   A12 GLU B  77  GLU B  82 -1  N  GLU B  82   O  GLN B  86           
SITE     1 AC1 12 ASN A 115  VAL A 119  THR A 129  ARG A 161                    
SITE     2 AC1 12 PHE B  99  ALA B 105  ARG B 106  GLY B 107                    
SITE     3 AC1 12 PHE B 136  THR B 137  ARG B 138  GLN B 139                    
SITE     1 AC2 13 PHE A  99  ALA A 105  ARG A 106  GLY A 107                    
SITE     2 AC2 13 HIS A 108  PHE A 136  THR A 137  ARG A 138                    
SITE     3 AC2 13 GLN A 139  ASN B 115  VAL B 119  LEU B 128                    
SITE     4 AC2 13 THR B 129                                                     
CRYST1   89.441   89.441  162.166  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011181  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011181  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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