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Database: PDB
Entry: 2F41
LinkDB: 2F41
Original site: 2F41 
HEADER    GENE REGULATION                         22-NOV-05   2F41              
TITLE     CRYSTAL STRUCTURE OF FAPR- A GLOBAL REGULATOR OF FATTY ACID           
TITLE    2 BIOSYNTHESIS IN B. SUBTILIS                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR FAPR;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: C-TEMINAL DOMAIN (RESIDUES 68-188);                        
COMPND   5 SYNONYM: FATTY ACID AND PHOSPHOLIPID BIOSYNTHESIS                    
COMPND   6 REGULATOR;                                                           
COMPND   7 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, GENE REGULATION                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BUSCHIAZZO,M.E.GUERIN,P.M.ALZARI                                    
REVDAT   2   24-FEB-09 2F41    1       VERSN                                    
REVDAT   1   31-OCT-06 2F41    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14035                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 790                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 528                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2964                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.70000                                             
REMARK   3    B22 (A**2) : 11.16000                                             
REMARK   3    B33 (A**2) : -6.45000                                             
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): 0.707         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.346         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.204         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.696        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2991 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2933 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4077 ; 1.826 ; 1.913       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6656 ; 0.955 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   419 ; 7.928 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;37.705 ;23.400       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   401 ;18.121 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;28.418 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   531 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3465 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   618 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   495 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2715 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1452 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1991 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    75 ; 0.136 ; 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):    10 ; 0.145 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    25 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.016 ; 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):  2630 ; 1.109 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   892 ; 0.193 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3294 ; 1.301 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   969 ; 1.980 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   783 ; 3.113 ; 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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     73       A      98      2                      
REMARK   3           1     B     73       B      98      2                      
REMARK   3           1     C     73       C      98      2                      
REMARK   3           1     D     73       D      98      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    101 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    101 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    101 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    101 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    165 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    165 ;  0.51 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    165 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    165 ;  0.32 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    101 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    101 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    101 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):    101 ;  0.12 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    165 ;  0.39 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    165 ;  0.40 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    165 ;  0.32 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    165 ;  0.37 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    105       A     155      2                      
REMARK   3           1     B    105       B     155      2                      
REMARK   3           1     C    105       C     155      2                      
REMARK   3           1     D    105       D     155      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    250 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    B    (A):    250 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    250 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    250 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    318 ;  0.26 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    318 ;  0.25 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    318 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    318 ;  0.26 ;  0.50           
REMARK   3   TIGHT THERMAL      2    A (A**2):    250 ;  0.13 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):    250 ;  0.13 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):    250 ;  0.13 ;  0.50           
REMARK   3   TIGHT THERMAL      2    D (A**2):    250 ;  0.12 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    318 ;  0.55 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    318 ;  0.60 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    318 ;  0.67 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    318 ;  0.71 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    161       A     183      2                      
REMARK   3           1     B    161       B     183      2                      
REMARK   3           1     C    161       C     183      2                      
REMARK   3           1     D    161       D     183      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    124 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):    124 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):    124 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    D    (A):    124 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    182 ;  0.30 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):    182 ;  0.30 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):    182 ;  0.40 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    D    (A):    182 ;  0.30 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):    124 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):    124 ;  0.14 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):    124 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      3    D (A**2):    124 ;  0.15 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    182 ;  0.55 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    B (A**2):    182 ;  0.49 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    C (A**2):    182 ;  0.49 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    D (A**2):    182 ;  0.53 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     98       A     104      6                      
REMARK   3           1     B     98       B     104      6                      
REMARK   3           1     D     98       D     104      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   4    A    (A):     77 ;  1.64 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    B    (A):     77 ;  1.08 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    D    (A):     77 ;  0.85 ;  5.00           
REMARK   3   LOOSE THERMAL      4    A (A**2):     77 ;  2.56 ; 10.00           
REMARK   3   LOOSE THERMAL      4    B (A**2):     77 ;  1.24 ; 10.00           
REMARK   3   LOOSE THERMAL      4    D (A**2):     77 ;  1.63 ; 10.00           
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 2F41 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 RCSB035425.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07175                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL-CUT                 
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14880                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.5                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 50.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.28700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
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   (%): 48.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULFATE, 2% PEG 400,       
REMARK 280  0.1M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.61950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.69250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.16000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.69250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.61950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.16000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 ASYMMETRIC UNIT CONTAINS TWO DIMERS. THE BIOLOGICAL      
REMARK 300 UNIT IS A DIMER.                                                     
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    68                                                      
REMARK 465     LEU A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     LEU A    71                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     ASP A   123                                                      
REMARK 465     ASP A   124                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     HIS A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     SER B    68                                                      
REMARK 465     LEU B    69                                                      
REMARK 465     SER B    70                                                      
REMARK 465     LEU B    71                                                      
REMARK 465     ASP B    72                                                      
REMARK 465     ASP B   123                                                      
REMARK 465     ASP B   124                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     SER B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     HIS B   187                                                      
REMARK 465     SER B   188                                                      
REMARK 465     SER C    68                                                      
REMARK 465     LEU C    69                                                      
REMARK 465     SER C    70                                                      
REMARK 465     LEU C    71                                                      
REMARK 465     ASP C    72                                                      
REMARK 465     PHE C    99                                                      
REMARK 465     SER C   100                                                      
REMARK 465     ARG C   101                                                      
REMARK 465     ASN C   102                                                      
REMARK 465     GLN C   103                                                      
REMARK 465     ILE C   104                                                      
REMARK 465     ASP C   123                                                      
REMARK 465     ASP C   124                                                      
REMARK 465     GLU C   125                                                      
REMARK 465     SER C   185                                                      
REMARK 465     LYS C   186                                                      
REMARK 465     HIS C   187                                                      
REMARK 465     SER C   188                                                      
REMARK 465     SER D    68                                                      
REMARK 465     LEU D    69                                                      
REMARK 465     SER D    70                                                      
REMARK 465     LEU D    71                                                      
REMARK 465     ASP D    72                                                      
REMARK 465     ASP D   123                                                      
REMARK 465     ASP D   124                                                      
REMARK 465     GLU D   125                                                      
REMARK 465     ARG D   184                                                      
REMARK 465     SER D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     HIS D   187                                                      
REMARK 465     SER D   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     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  77    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  80    CG   OD1  OD2                                       
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  92    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLN A  95    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 103    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     LEU A 128    CG   CD1  CD2                                       
REMARK 470     ASP A 133    CG   OD1  OD2                                       
REMARK 470     ARG A 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 141    CG   CD   CE   NZ                                   
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 145    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     ARG A 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 183    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  92    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     ARG B 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 126    CG   CD1  CD2                                       
REMARK 470     LEU B 128    CG   CD1  CD2                                       
REMARK 470     ARG B 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 141    CG   CD   CE   NZ                                   
REMARK 470     ARG B 145    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 151    CG   CD   CE   NZ                                   
REMARK 470     GLU B 156    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 157    CB   CG   CD   CE   NZ                              
REMARK 470     GLU B 158    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     ARG B 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 172    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  73    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU C  77    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  80    CG   OD1  OD2                                       
REMARK 470     GLU C  82    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  84    CG   OD1  OD2                                       
REMARK 470     ASP C  85    CG   OD1  OD2                                       
REMARK 470     GLN C  86    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  92    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  94    CG   CD   CE   NZ                                   
REMARK 470     GLN C  95    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  96    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 126    CG   CD1  CD2                                       
REMARK 470     LEU C 128    CG   CD1  CD2                                       
REMARK 470     ASP C 133    CG   OD1  OD2                                       
REMARK 470     ARG C 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 141    CG   CD   CE   NZ                                   
REMARK 470     ARG C 145    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 151    CG   CD   CE   NZ                                   
REMARK 470     LYS C 157    CG   CD   CE   NZ                                   
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 159    CG   CD   CE   NZ                                   
REMARK 470     GLU C 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 172    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 183    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU D  73    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU D  77    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  82    CG   CD   OE1  OE2                                  
REMARK 470     ASP D  84    CG   OD1  OD2                                       
REMARK 470     ASP D  85    CG   OD1  OD2                                       
REMARK 470     GLN D  86    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  92    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  96    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 126    CG   CD1  CD2                                       
REMARK 470     LEU D 128    CG   CD1  CD2                                       
REMARK 470     SER D 131    OG                                                  
REMARK 470     ASP D 133    CG   OD1  OD2                                       
REMARK 470     ARG D 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 141    CG   CD   CE   NZ                                   
REMARK 470     LYS D 151    CG   CD   CE   NZ                                   
REMARK 470     GLU D 156    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 157    CG   CD   CE   NZ                                   
REMARK 470     GLU D 158    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 159    CG   CD   CE   NZ                                   
REMARK 470     ARG D 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 172    CG   CD   OE1  OE2                                  
REMARK 470     TYR D 183    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    ASP A  84       18.60     57.35                                   
REMARK 500    ASP A  85      -60.44   -129.65                                   
REMARK 500    GLU A 158      -78.36    -48.76                                   
REMARK 500    ASP B  85      -75.51   -145.73                                   
REMARK 500    LYS B  94     -166.91   -111.56                                   
REMARK 500    THR B 137      -72.73    -97.44                                   
REMARK 500    GLU B 158      -91.78    -27.15                                   
REMARK 500    LYS B 159        8.32    -67.84                                   
REMARK 500    ASP C  84       19.78     35.48                                   
REMARK 500    ASP C  85      -79.62   -116.11                                   
REMARK 500    LYS C 157     -139.51     49.92                                   
REMARK 500    ASP D  84       -1.66     74.49                                   
REMARK 500    ASP D  85      -68.79   -120.11                                   
REMARK 500    GLU D  96      -27.77    -39.14                                   
REMARK 500    SER D 100      -77.77    -23.97                                   
REMARK 500    THR D 137      -70.74    -93.97                                   
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 GLU A  156     LYS A  157                  148.21                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F3X   RELATED DB: PDB                                   
REMARK 900 FAPR IN COMPLEX WITH MALONYL-COA                                     
DBREF  2F41 A   68   188  UNP    O34835   FAPR_BACSU      68    188             
DBREF  2F41 B   68   188  UNP    O34835   FAPR_BACSU      68    188             
DBREF  2F41 C   68   188  UNP    O34835   FAPR_BACSU      68    188             
DBREF  2F41 D   68   188  UNP    O34835   FAPR_BACSU      68    188             
SEQRES   1 A  121  SER LEU SER LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP          
SEQRES   2 A  121  LEU GLU LEU ASP ASP GLN ALA ILE SER ILE LEU GLU ILE          
SEQRES   3 A  121  LYS GLN GLU HIS VAL PHE SER ARG ASN GLN ILE ALA ARG          
SEQRES   4 A  121  GLY HIS HIS LEU PHE ALA GLN ALA ASN SER LEU ALA VAL          
SEQRES   5 A  121  ALA VAL ILE ASP ASP GLU LEU ALA LEU THR ALA SER ALA          
SEQRES   6 A  121  ASP ILE ARG PHE THR ARG GLN VAL LYS GLN GLY GLU ARG          
SEQRES   7 A  121  VAL VAL ALA LYS ALA LYS VAL THR ALA VAL GLU LYS GLU          
SEQRES   8 A  121  LYS GLY ARG THR VAL VAL GLU VAL ASN SER TYR VAL GLY          
SEQRES   9 A  121  GLU GLU ILE VAL PHE SER GLY ARG PHE ASP MET TYR ARG          
SEQRES  10 A  121  SER LYS HIS SER                                              
SEQRES   1 B  121  SER LEU SER LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP          
SEQRES   2 B  121  LEU GLU LEU ASP ASP GLN ALA ILE SER ILE LEU GLU ILE          
SEQRES   3 B  121  LYS GLN GLU HIS VAL PHE SER ARG ASN GLN ILE ALA ARG          
SEQRES   4 B  121  GLY HIS HIS LEU PHE ALA GLN ALA ASN SER LEU ALA VAL          
SEQRES   5 B  121  ALA VAL ILE ASP ASP GLU LEU ALA LEU THR ALA SER ALA          
SEQRES   6 B  121  ASP ILE ARG PHE THR ARG GLN VAL LYS GLN GLY GLU ARG          
SEQRES   7 B  121  VAL VAL ALA LYS ALA LYS VAL THR ALA VAL GLU LYS GLU          
SEQRES   8 B  121  LYS GLY ARG THR VAL VAL GLU VAL ASN SER TYR VAL GLY          
SEQRES   9 B  121  GLU GLU ILE VAL PHE SER GLY ARG PHE ASP MET TYR ARG          
SEQRES  10 B  121  SER LYS HIS SER                                              
SEQRES   1 C  121  SER LEU SER LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP          
SEQRES   2 C  121  LEU GLU LEU ASP ASP GLN ALA ILE SER ILE LEU GLU ILE          
SEQRES   3 C  121  LYS GLN GLU HIS VAL PHE SER ARG ASN GLN ILE ALA ARG          
SEQRES   4 C  121  GLY HIS HIS LEU PHE ALA GLN ALA ASN SER LEU ALA VAL          
SEQRES   5 C  121  ALA VAL ILE ASP ASP GLU LEU ALA LEU THR ALA SER ALA          
SEQRES   6 C  121  ASP ILE ARG PHE THR ARG GLN VAL LYS GLN GLY GLU ARG          
SEQRES   7 C  121  VAL VAL ALA LYS ALA LYS VAL THR ALA VAL GLU LYS GLU          
SEQRES   8 C  121  LYS GLY ARG THR VAL VAL GLU VAL ASN SER TYR VAL GLY          
SEQRES   9 C  121  GLU GLU ILE VAL PHE SER GLY ARG PHE ASP MET TYR ARG          
SEQRES  10 C  121  SER LYS HIS SER                                              
SEQRES   1 D  121  SER LEU SER LEU ASP GLU VAL ILE GLY GLU ILE ILE ASP          
SEQRES   2 D  121  LEU GLU LEU ASP ASP GLN ALA ILE SER ILE LEU GLU ILE          
SEQRES   3 D  121  LYS GLN GLU HIS VAL PHE SER ARG ASN GLN ILE ALA ARG          
SEQRES   4 D  121  GLY HIS HIS LEU PHE ALA GLN ALA ASN SER LEU ALA VAL          
SEQRES   5 D  121  ALA VAL ILE ASP ASP GLU LEU ALA LEU THR ALA SER ALA          
SEQRES   6 D  121  ASP ILE ARG PHE THR ARG GLN VAL LYS GLN GLY GLU ARG          
SEQRES   7 D  121  VAL VAL ALA LYS ALA LYS VAL THR ALA VAL GLU LYS GLU          
SEQRES   8 D  121  LYS GLY ARG THR VAL VAL GLU VAL ASN SER TYR VAL GLY          
SEQRES   9 D  121  GLU GLU ILE VAL PHE SER GLY ARG PHE ASP MET TYR ARG          
SEQRES  10 D  121  SER LYS HIS SER                                              
FORMUL   5  HOH   *8(H2 O)                                                      
HELIX    1   1 ARG A  106  VAL A  121  1                                  16    
HELIX    2   2 ARG B  106  VAL B  121  1                                  16    
HELIX    3   3 ARG C  106  VAL C  121  1                                  16    
HELIX    4   4 ARG D  106  VAL D  121  1                                  16    
SHEET    1   A 4 ALA A  87  ILE A  90  0                                        
SHEET    2   A 4 VAL A 147  ALA A 150 -1  O  ALA A 150   N  ALA A  87           
SHEET    3   A 4 VAL A 163  TYR A 169 -1  O  ASN A 167   N  LYS A 149           
SHEET    4   A 4 ILE A 174  ASP A 181 -1  O  PHE A 180   N  VAL A 164           
SHEET    1   B 7 SER A 131  ALA A 132  0                                        
SHEET    2   B 7 SER B 131  PHE B 136 -1  O  ILE B 134   N  ALA A 132           
SHEET    3   B 7 ILE B 174  ASP B 181 -1  O  ASP B 181   N  SER B 131           
SHEET    4   B 7 VAL B 163  TYR B 169 -1  N  VAL B 164   O  PHE B 180           
SHEET    5   B 7 VAL B 147  ALA B 150 -1  N  VAL B 147   O  TYR B 169           
SHEET    6   B 7 ALA B  87  ILE B  90 -1  N  ALA B  87   O  ALA B 150           
SHEET    7   B 7 GLU B  77  ASP B  80 -1  N  ILE B  79   O  ILE B  88           
SHEET    1   C 4 ILE C  88  ILE C  90  0                                        
SHEET    2   C 4 VAL C 147  LYS C 149 -1  O  ALA C 148   N  SER C  89           
SHEET    3   C 4 THR C 162  TYR C 169 -1  O  TYR C 169   N  VAL C 147           
SHEET    4   C 4 ALA C 154  VAL C 155 -1  N  ALA C 154   O  VAL C 163           
SHEET    1   D 4 ILE C  88  ILE C  90  0                                        
SHEET    2   D 4 VAL C 147  LYS C 149 -1  O  ALA C 148   N  SER C  89           
SHEET    3   D 4 THR C 162  TYR C 169 -1  O  TYR C 169   N  VAL C 147           
SHEET    4   D 4 ILE C 174  MET C 182 -1  O  MET C 182   N  THR C 162           
SHEET    1   E 5 ILE D  88  LEU D  91  0                                        
SHEET    2   E 5 VAL D 146  LYS D 149 -1  O  ALA D 148   N  SER D  89           
SHEET    3   E 5 VAL D 163  TYR D 169 -1  O  ASN D 167   N  LYS D 149           
SHEET    4   E 5 ILE D 174  ASP D 181 -1  O  PHE D 180   N  VAL D 164           
SHEET    5   E 5 ARG D 135  PHE D 136 -1  N  ARG D 135   O  SER D 177           
CRYST1   39.239   84.320  155.385  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025485  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006436        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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