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Database: PDB
Entry: 4ALL
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HEADER    OXIDOREDUCTASE                          04-MAR-12   4ALL              
TITLE     CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP              
TITLE    2 AND TRICLOSAN (P212121)                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADPH];            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ENR, ENOYL-ACP REDUCTASE;                                   
COMPND   5 EC: 1.3.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: N315;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-16B                                   
KEYWDS    OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE SUPERFAMILY,      
KEYWDS   2 FATTY ACID BIOSYNTHESIS, LIPID SYNTHESIS                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHIEBEL,A.CHANG,P.J.TONGE,C.KISKER                                 
REVDAT   2   23-MAY-12 4ALL    1       JRNL                                     
REVDAT   1   09-MAY-12 4ALL    0                                                
JRNL        AUTH   J.SCHIEBEL,A.CHANG,H.LU,M.V.BAXTER,P.J.TONGE,C.KISKER        
JRNL        TITL   STAPHYLOCOCCUS AUREUS FABI: INHIBITION, SUBSTRATE            
JRNL        TITL 2 RECOGNITION AND POTENTIAL IMPLICATIONS FOR IN VIVO           
JRNL        TITL 3 ESSENTIALITY                                                 
JRNL        REF    STRUCTURE                     V.  20   802 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22579249                                                     
JRNL        DOI    10.1016/J.STR.2012.03.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.89                          
REMARK   3   NUMBER OF REFLECTIONS             : 21537                          
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) : 0.21645                         
REMARK   3   R VALUE            (WORKING SET) : 0.21406                         
REMARK   3   FREE R VALUE                     : 0.26240                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1146                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.873                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1606                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.323                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.346                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7832                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 260                                     
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.354                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34                                                
REMARK   3    B22 (A**2) : -2.33                                                
REMARK   3    B33 (A**2) : 2.67                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.482         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.384         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.894        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8220 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11125 ; 1.591 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1014 ; 5.908 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   364 ;39.299 ;25.055       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1433 ;18.412 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;16.409 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1255 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6088 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5014 ; 0.359 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8020 ; 0.696 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3206 ; 1.244 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3105 ; 2.244 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A      98      2                      
REMARK   3           1     B      2       B      98      2                      
REMARK   3           1     C      2       C      98      2                      
REMARK   3           1     D      2       D      98      2                      
REMARK   3           2     A    100       A     256      2                      
REMARK   3           2     B    100       B     256      2                      
REMARK   3           2     C    100       C     256      2                      
REMARK   3           2     D    100       D     256      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1012 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1012 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1012 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1012 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    934 ;  0.08 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    934 ;  0.06 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    934 ;  0.07 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    934 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1012 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1012 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1012 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1012 ;  0.08 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    934 ;  0.10 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    934 ;  0.09 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    934 ;  0.09 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    934 ;  0.09 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8152 -29.1101 -25.2183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3861 T22:   0.0923                                     
REMARK   3      T33:   1.3506 T12:  -0.0499                                     
REMARK   3      T13:   0.0607 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3134 L22:   3.3470                                     
REMARK   3      L33:   2.0778 L12:  -0.8241                                     
REMARK   3      L13:   0.3320 L23:   0.1234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0827 S12:  -0.1149 S13:   0.9493                       
REMARK   3      S21:  -0.1883 S22:  -0.1477 S23:  -0.8049                       
REMARK   3      S31:  -0.1369 S32:   0.3693 S33:   0.0651                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   256                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4078 -35.2356 -39.5374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6068 T22:   0.1947                                     
REMARK   3      T33:   0.8623 T12:   0.0237                                     
REMARK   3      T13:  -0.0713 T23:   0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3745 L22:   3.3631                                     
REMARK   3      L33:   2.3991 L12:  -0.1977                                     
REMARK   3      L13:   0.4589 L23:  -0.2702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1857 S12:   0.5619 S13:   0.2859                       
REMARK   3      S21:  -0.9327 S22:  -0.0836 S23:   0.2479                       
REMARK   3      S31:   0.0618 S32:  -0.3076 S33:  -0.1021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   256                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5068 -45.8456 -10.8043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3891 T22:   0.4041                                     
REMARK   3      T33:   0.9734 T12:  -0.0879                                     
REMARK   3      T13:   0.0806 T23:  -0.0750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2835 L22:   3.3742                                     
REMARK   3      L33:   1.9688 L12:  -0.6677                                     
REMARK   3      L13:  -0.3332 L23:  -0.1041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:  -0.6631 S13:   0.1401                       
REMARK   3      S21:   0.4012 S22:   0.0988 S23:   0.6840                       
REMARK   3      S31:   0.1825 S32:  -0.4179 S33:  -0.0758                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0677 -54.0536  -6.4677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5430 T22:   0.3583                                     
REMARK   3      T33:   0.8568 T12:   0.0340                                     
REMARK   3      T13:  -0.0630 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3782 L22:   2.5340                                     
REMARK   3      L33:   2.9338 L12:  -0.3548                                     
REMARK   3      L13:  -0.4827 L23:   0.2865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.9987 S13:  -0.0926                       
REMARK   3      S21:   0.4269 S22:  -0.0532 S23:  -0.1826                       
REMARK   3      S31:   0.3815 S32:   0.3089 S33:   0.0244                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4ALL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51457.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22827                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.91                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY                : 5.25                               
REMARK 200  R MERGE                    (I) : 0.15                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.49                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.16                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.51                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2QIO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 46.11                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M K/NA-PHOSPHATE PH 6.5,             
REMARK 280  35% MPD                                                             
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       41.76000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.82000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.95500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.82000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.76000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.95500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.1 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     ILE A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ARG A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     ILE B    -4                                                      
REMARK 465     GLU B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     MET C   -20                                                      
REMARK 465     GLY C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     GLY C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     ILE C    -4                                                      
REMARK 465     GLU C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     ARG C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     MET D   -20                                                      
REMARK 465     GLY D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     ILE D    -4                                                      
REMARK 465     GLU D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     ARG D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A   102     O    HOH A  2001              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   112     NH2  ARG D    18     3554     2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   2   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ARG A  43   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A  45   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG B  45   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG B 103   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG B 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG C  45   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG C 103   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG C 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG D  45   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG D  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG D 103   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG D 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A   2     -165.22    -59.76                                   
REMARK 500    ASN A   3      -81.96   -101.14                                   
REMARK 500    ASN A  56       62.75   -115.43                                   
REMARK 500    SER A 122      -67.36   -121.08                                   
REMARK 500    ASN A 158     -110.77     32.13                                   
REMARK 500    ASP A 249       33.39   -153.02                                   
REMARK 500    SER A 250       14.30     54.06                                   
REMARK 500    ARG B  43       -8.91    -56.26                                   
REMARK 500    ASN B  56       63.71   -114.02                                   
REMARK 500    SER B 122      -56.90   -120.33                                   
REMARK 500    ASN B 158     -111.09     37.79                                   
REMARK 500    ASP B 249       28.50   -153.21                                   
REMARK 500    GLU C   5      150.99    -48.63                                   
REMARK 500    ASN C   6        7.91     58.45                                   
REMARK 500    ASN C  56       64.36   -112.89                                   
REMARK 500    SER C 122      -61.67   -124.81                                   
REMARK 500    ASN C 158     -111.54     36.87                                   
REMARK 500    ASP C 249       27.82   -153.59                                   
REMARK 500    ARG D  43       -9.14    -56.92                                   
REMARK 500    ASN D  56       61.89   -115.18                                   
REMARK 500    SER D 122      -60.90   -123.42                                   
REMARK 500    ASN D 158     -120.20     35.22                                   
REMARK 500    ASP D 249       30.27   -151.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A   3        21.8      L          L   OUTSIDE RANGE           
REMARK 500    MET D  99        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL A1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL D1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL B1258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL C1258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D1258                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ALI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH                 
REMARK 900  NADP AND TRICLOSAN (P1)                                             
REMARK 900 RELATED ID: 4ALJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH                 
REMARK 900  NADP AND 5-CHLORO-2-PHENOXYPHENOL                                   
REMARK 900 RELATED ID: 4ALK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH                 
REMARK 900  NADP AND 5-ETHYL-2-PHENOXYPHENOL                                    
REMARK 900 RELATED ID: 4ALM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS FABI (P43212)                        
REMARK 900 RELATED ID: 4ALN   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS FABI (P32)                           
DBREF  4ALL A    1   256  UNP    Q7A6D8   Q7A6D8_STAAN     1    256             
DBREF  4ALL B    1   256  UNP    Q7A6D8   Q7A6D8_STAAN     1    256             
DBREF  4ALL C    1   256  UNP    Q7A6D8   Q7A6D8_STAAN     1    256             
DBREF  4ALL D    1   256  UNP    Q7A6D8   Q7A6D8_STAAN     1    256             
SEQADV 4ALL MET A  -20  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY A  -19  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -18  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -17  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -16  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -15  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -14  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -13  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -12  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -11  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A  -10  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A   -9  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER A   -8  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER A   -7  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY A   -6  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A   -5  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ILE A   -4  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLU A   -3  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY A   -2  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ARG A   -1  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS A    0  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL MET B  -20  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY B  -19  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -18  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -17  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -16  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -15  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -14  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -13  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -12  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -11  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B  -10  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B   -9  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER B   -8  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER B   -7  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY B   -6  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B   -5  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ILE B   -4  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLU B   -3  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY B   -2  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ARG B   -1  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS B    0  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL MET C  -20  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY C  -19  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -18  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -17  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -16  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -15  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -14  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -13  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -12  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -11  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C  -10  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C   -9  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER C   -8  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER C   -7  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY C   -6  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C   -5  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ILE C   -4  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLU C   -3  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY C   -2  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ARG C   -1  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS C    0  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL MET D  -20  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY D  -19  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -18  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -17  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -16  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -15  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -14  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -13  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -12  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -11  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D  -10  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D   -9  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER D   -8  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL SER D   -7  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY D   -6  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D   -5  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ILE D   -4  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLU D   -3  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL GLY D   -2  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL ARG D   -1  UNP  Q7A6D8              EXPRESSION TAG                 
SEQADV 4ALL HIS D    0  UNP  Q7A6D8              EXPRESSION TAG                 
SEQRES   1 A  277  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 A  277  SER GLY HIS ILE GLU GLY ARG HIS MET LEU ASN LEU GLU          
SEQRES   3 A  277  ASN LYS THR TYR VAL ILE MET GLY ILE ALA ASN LYS ARG          
SEQRES   4 A  277  SER ILE ALA PHE GLY VAL ALA LYS VAL LEU ASP GLN LEU          
SEQRES   5 A  277  GLY ALA LYS LEU VAL PHE THR TYR ARG LYS GLU ARG SER          
SEQRES   6 A  277  ARG LYS GLU LEU GLU LYS LEU LEU GLU GLN LEU ASN GLN          
SEQRES   7 A  277  PRO GLU ALA HIS LEU TYR GLN ILE ASP VAL GLN SER ASP          
SEQRES   8 A  277  GLU GLU VAL ILE ASN GLY PHE GLU GLN ILE GLY LYS ASP          
SEQRES   9 A  277  VAL GLY ASN ILE ASP GLY VAL TYR HIS SER ILE ALA PHE          
SEQRES  10 A  277  ALA ASN MET GLU ASP LEU ARG GLY ARG PHE SER GLU THR          
SEQRES  11 A  277  SER ARG GLU GLY PHE LEU LEU ALA GLN ASP ILE SER SER          
SEQRES  12 A  277  TYR SER LEU THR ILE VAL ALA HIS GLU ALA LYS LYS LEU          
SEQRES  13 A  277  MET PRO GLU GLY GLY SER ILE VAL ALA THR THR TYR LEU          
SEQRES  14 A  277  GLY GLY GLU PHE ALA VAL GLN ASN TYR ASN VAL MET GLY          
SEQRES  15 A  277  VAL ALA LYS ALA SER LEU GLU ALA ASN VAL LYS TYR LEU          
SEQRES  16 A  277  ALA LEU ASP LEU GLY PRO ASP ASN ILE ARG VAL ASN ALA          
SEQRES  17 A  277  ILE SER ALA GLY PRO ILE ARG THR LEU SER ALA LYS GLY          
SEQRES  18 A  277  VAL GLY GLY PHE ASN THR ILE LEU LYS GLU ILE GLU GLU          
SEQRES  19 A  277  ARG ALA PRO LEU LYS ARG ASN VAL ASP GLN VAL GLU VAL          
SEQRES  20 A  277  GLY LYS THR ALA ALA TYR LEU LEU SER ASP LEU SER SER          
SEQRES  21 A  277  GLY VAL THR GLY GLU ASN ILE HIS VAL ASP SER GLY PHE          
SEQRES  22 A  277  HIS ALA ILE LYS                                              
SEQRES   1 B  277  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 B  277  SER GLY HIS ILE GLU GLY ARG HIS MET LEU ASN LEU GLU          
SEQRES   3 B  277  ASN LYS THR TYR VAL ILE MET GLY ILE ALA ASN LYS ARG          
SEQRES   4 B  277  SER ILE ALA PHE GLY VAL ALA LYS VAL LEU ASP GLN LEU          
SEQRES   5 B  277  GLY ALA LYS LEU VAL PHE THR TYR ARG LYS GLU ARG SER          
SEQRES   6 B  277  ARG LYS GLU LEU GLU LYS LEU LEU GLU GLN LEU ASN GLN          
SEQRES   7 B  277  PRO GLU ALA HIS LEU TYR GLN ILE ASP VAL GLN SER ASP          
SEQRES   8 B  277  GLU GLU VAL ILE ASN GLY PHE GLU GLN ILE GLY LYS ASP          
SEQRES   9 B  277  VAL GLY ASN ILE ASP GLY VAL TYR HIS SER ILE ALA PHE          
SEQRES  10 B  277  ALA ASN MET GLU ASP LEU ARG GLY ARG PHE SER GLU THR          
SEQRES  11 B  277  SER ARG GLU GLY PHE LEU LEU ALA GLN ASP ILE SER SER          
SEQRES  12 B  277  TYR SER LEU THR ILE VAL ALA HIS GLU ALA LYS LYS LEU          
SEQRES  13 B  277  MET PRO GLU GLY GLY SER ILE VAL ALA THR THR TYR LEU          
SEQRES  14 B  277  GLY GLY GLU PHE ALA VAL GLN ASN TYR ASN VAL MET GLY          
SEQRES  15 B  277  VAL ALA LYS ALA SER LEU GLU ALA ASN VAL LYS TYR LEU          
SEQRES  16 B  277  ALA LEU ASP LEU GLY PRO ASP ASN ILE ARG VAL ASN ALA          
SEQRES  17 B  277  ILE SER ALA GLY PRO ILE ARG THR LEU SER ALA LYS GLY          
SEQRES  18 B  277  VAL GLY GLY PHE ASN THR ILE LEU LYS GLU ILE GLU GLU          
SEQRES  19 B  277  ARG ALA PRO LEU LYS ARG ASN VAL ASP GLN VAL GLU VAL          
SEQRES  20 B  277  GLY LYS THR ALA ALA TYR LEU LEU SER ASP LEU SER SER          
SEQRES  21 B  277  GLY VAL THR GLY GLU ASN ILE HIS VAL ASP SER GLY PHE          
SEQRES  22 B  277  HIS ALA ILE LYS                                              
SEQRES   1 C  277  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 C  277  SER GLY HIS ILE GLU GLY ARG HIS MET LEU ASN LEU GLU          
SEQRES   3 C  277  ASN LYS THR TYR VAL ILE MET GLY ILE ALA ASN LYS ARG          
SEQRES   4 C  277  SER ILE ALA PHE GLY VAL ALA LYS VAL LEU ASP GLN LEU          
SEQRES   5 C  277  GLY ALA LYS LEU VAL PHE THR TYR ARG LYS GLU ARG SER          
SEQRES   6 C  277  ARG LYS GLU LEU GLU LYS LEU LEU GLU GLN LEU ASN GLN          
SEQRES   7 C  277  PRO GLU ALA HIS LEU TYR GLN ILE ASP VAL GLN SER ASP          
SEQRES   8 C  277  GLU GLU VAL ILE ASN GLY PHE GLU GLN ILE GLY LYS ASP          
SEQRES   9 C  277  VAL GLY ASN ILE ASP GLY VAL TYR HIS SER ILE ALA PHE          
SEQRES  10 C  277  ALA ASN MET GLU ASP LEU ARG GLY ARG PHE SER GLU THR          
SEQRES  11 C  277  SER ARG GLU GLY PHE LEU LEU ALA GLN ASP ILE SER SER          
SEQRES  12 C  277  TYR SER LEU THR ILE VAL ALA HIS GLU ALA LYS LYS LEU          
SEQRES  13 C  277  MET PRO GLU GLY GLY SER ILE VAL ALA THR THR TYR LEU          
SEQRES  14 C  277  GLY GLY GLU PHE ALA VAL GLN ASN TYR ASN VAL MET GLY          
SEQRES  15 C  277  VAL ALA LYS ALA SER LEU GLU ALA ASN VAL LYS TYR LEU          
SEQRES  16 C  277  ALA LEU ASP LEU GLY PRO ASP ASN ILE ARG VAL ASN ALA          
SEQRES  17 C  277  ILE SER ALA GLY PRO ILE ARG THR LEU SER ALA LYS GLY          
SEQRES  18 C  277  VAL GLY GLY PHE ASN THR ILE LEU LYS GLU ILE GLU GLU          
SEQRES  19 C  277  ARG ALA PRO LEU LYS ARG ASN VAL ASP GLN VAL GLU VAL          
SEQRES  20 C  277  GLY LYS THR ALA ALA TYR LEU LEU SER ASP LEU SER SER          
SEQRES  21 C  277  GLY VAL THR GLY GLU ASN ILE HIS VAL ASP SER GLY PHE          
SEQRES  22 C  277  HIS ALA ILE LYS                                              
SEQRES   1 D  277  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 D  277  SER GLY HIS ILE GLU GLY ARG HIS MET LEU ASN LEU GLU          
SEQRES   3 D  277  ASN LYS THR TYR VAL ILE MET GLY ILE ALA ASN LYS ARG          
SEQRES   4 D  277  SER ILE ALA PHE GLY VAL ALA LYS VAL LEU ASP GLN LEU          
SEQRES   5 D  277  GLY ALA LYS LEU VAL PHE THR TYR ARG LYS GLU ARG SER          
SEQRES   6 D  277  ARG LYS GLU LEU GLU LYS LEU LEU GLU GLN LEU ASN GLN          
SEQRES   7 D  277  PRO GLU ALA HIS LEU TYR GLN ILE ASP VAL GLN SER ASP          
SEQRES   8 D  277  GLU GLU VAL ILE ASN GLY PHE GLU GLN ILE GLY LYS ASP          
SEQRES   9 D  277  VAL GLY ASN ILE ASP GLY VAL TYR HIS SER ILE ALA PHE          
SEQRES  10 D  277  ALA ASN MET GLU ASP LEU ARG GLY ARG PHE SER GLU THR          
SEQRES  11 D  277  SER ARG GLU GLY PHE LEU LEU ALA GLN ASP ILE SER SER          
SEQRES  12 D  277  TYR SER LEU THR ILE VAL ALA HIS GLU ALA LYS LYS LEU          
SEQRES  13 D  277  MET PRO GLU GLY GLY SER ILE VAL ALA THR THR TYR LEU          
SEQRES  14 D  277  GLY GLY GLU PHE ALA VAL GLN ASN TYR ASN VAL MET GLY          
SEQRES  15 D  277  VAL ALA LYS ALA SER LEU GLU ALA ASN VAL LYS TYR LEU          
SEQRES  16 D  277  ALA LEU ASP LEU GLY PRO ASP ASN ILE ARG VAL ASN ALA          
SEQRES  17 D  277  ILE SER ALA GLY PRO ILE ARG THR LEU SER ALA LYS GLY          
SEQRES  18 D  277  VAL GLY GLY PHE ASN THR ILE LEU LYS GLU ILE GLU GLU          
SEQRES  19 D  277  ARG ALA PRO LEU LYS ARG ASN VAL ASP GLN VAL GLU VAL          
SEQRES  20 D  277  GLY LYS THR ALA ALA TYR LEU LEU SER ASP LEU SER SER          
SEQRES  21 D  277  GLY VAL THR GLY GLU ASN ILE HIS VAL ASP SER GLY PHE          
SEQRES  22 D  277  HIS ALA ILE LYS                                              
HET    TCL  A1257      17                                                       
HET    NAP  A1258      48                                                       
HET    NAP  B1257      48                                                       
HET    TCL  D1257      17                                                       
HET    TCL  B1258      17                                                       
HET    NAP  C1257      48                                                       
HET    TCL  C1258      17                                                       
HET    NAP  D1258      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE                           
HETNAM   2 NAP  PHOSPHATE                                                       
HETNAM     TCL TRICLOSAN                                                        
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   5  NAP    4(C21 H28 N7 O17 P3)                                         
FORMUL   6  TCL    4(C12 H7 CL3 O2)                                             
FORMUL   7  HOH   *9(H2 O)                                                      
HELIX    1   1 SER A   19  LEU A   31  1                                  13    
HELIX    2   2 LYS A   41  ARG A   43  5                                   3    
HELIX    3   3 SER A   44  GLU A   53  1                                  10    
HELIX    4   4 SER A   69  GLY A   85  1                                  17    
HELIX    5   5 ARG A  105  THR A  109  5                                   5    
HELIX    6   6 SER A  110  SER A  122  1                                  13    
HELIX    7   7 SER A  122  LYS A  133  1                                  12    
HELIX    8   8 LYS A  134  MET A  136  5                                   3    
HELIX    9   9 GLY A  149  GLU A  151  5                                   3    
HELIX   10  10 TYR A  157  GLY A  179  1                                  23    
HELIX   11  11 LEU A  196  VAL A  201  5                                   6    
HELIX   12  12 GLY A  203  ALA A  215  1                                  13    
HELIX   13  13 ASP A  222  SER A  235  1                                  14    
HELIX   14  14 ASP A  236  SER A  239  5                                   4    
HELIX   15  15 GLY A  251  ALA A  254  5                                   4    
HELIX   16  16 SER B   19  LEU B   31  1                                  13    
HELIX   17  17 LYS B   41  ARG B   43  5                                   3    
HELIX   18  18 SER B   44  GLU B   53  1                                  10    
HELIX   19  19 SER B   69  GLY B   85  1                                  17    
HELIX   20  20 ARG B  105  THR B  109  5                                   5    
HELIX   21  21 SER B  110  SER B  122  1                                  13    
HELIX   22  22 SER B  122  LYS B  134  1                                  13    
HELIX   23  23 GLY B  149  GLU B  151  5                                   3    
HELIX   24  24 TYR B  157  GLY B  179  1                                  23    
HELIX   25  25 LEU B  196  VAL B  201  5                                   6    
HELIX   26  26 GLY B  203  ALA B  215  1                                  13    
HELIX   27  27 ASP B  222  SER B  235  1                                  14    
HELIX   28  28 ASP B  236  SER B  239  5                                   4    
HELIX   29  29 GLY B  251  ALA B  254  5                                   4    
HELIX   30  30 SER C   19  LEU C   31  1                                  13    
HELIX   31  31 LYS C   41  ARG C   43  5                                   3    
HELIX   32  32 SER C   44  GLU C   53  1                                  10    
HELIX   33  33 SER C   69  GLY C   85  1                                  17    
HELIX   34  34 ARG C  105  THR C  109  5                                   5    
HELIX   35  35 SER C  110  SER C  122  1                                  13    
HELIX   36  36 SER C  122  LYS C  134  1                                  13    
HELIX   37  37 GLY C  149  GLU C  151  5                                   3    
HELIX   38  38 TYR C  157  GLY C  179  1                                  23    
HELIX   39  39 LEU C  196  VAL C  201  5                                   6    
HELIX   40  40 GLY C  203  ALA C  215  1                                  13    
HELIX   41  41 ASP C  222  SER C  235  1                                  14    
HELIX   42  42 ASP C  236  SER C  239  5                                   4    
HELIX   43  43 GLY C  251  ALA C  254  5                                   4    
HELIX   44  44 SER D   19  LEU D   31  1                                  13    
HELIX   45  45 LYS D   41  ARG D   43  5                                   3    
HELIX   46  46 SER D   44  GLU D   53  1                                  10    
HELIX   47  47 SER D   69  GLY D   85  1                                  17    
HELIX   48  48 ARG D  105  THR D  109  5                                   5    
HELIX   49  49 SER D  110  SER D  122  1                                  13    
HELIX   50  50 SER D  122  LYS D  134  1                                  13    
HELIX   51  51 GLY D  149  GLU D  151  5                                   3    
HELIX   52  52 TYR D  157  GLY D  179  1                                  23    
HELIX   53  53 LEU D  196  VAL D  201  5                                   6    
HELIX   54  54 GLY D  203  ALA D  215  1                                  13    
HELIX   55  55 ASP D  222  SER D  235  1                                  14    
HELIX   56  56 ASP D  236  SER D  239  5                                   4    
HELIX   57  57 GLY D  251  ALA D  254  5                                   4    
SHEET    1  AA 7 LEU A  62  GLN A  64  0                                        
SHEET    2  AA 7 LYS A  34  TYR A  39  1  O  PHE A  37   N  TYR A  63           
SHEET    3  AA 7 THR A   8  MET A  12  1  O  TYR A   9   N  VAL A  36           
SHEET    4  AA 7 GLY A  89  HIS A  92  1  O  GLY A  89   N  VAL A  10           
SHEET    5  AA 7 GLY A 140  TYR A 147  1  O  SER A 141   N  VAL A  90           
SHEET    6  AA 7 ILE A 183  ALA A 190  1  O  ARG A 184   N  ILE A 142           
SHEET    7  AA 7 ASN A 245  VAL A 248  1  O  ILE A 246   N  SER A 189           
SHEET    1  BA 7 LEU B  62  GLN B  64  0                                        
SHEET    2  BA 7 LYS B  34  TYR B  39  1  O  PHE B  37   N  TYR B  63           
SHEET    3  BA 7 THR B   8  MET B  12  1  O  TYR B   9   N  VAL B  36           
SHEET    4  BA 7 GLY B  89  HIS B  92  1  O  GLY B  89   N  VAL B  10           
SHEET    5  BA 7 GLY B 140  TYR B 147  1  O  SER B 141   N  VAL B  90           
SHEET    6  BA 7 ILE B 183  ALA B 190  1  O  ARG B 184   N  ILE B 142           
SHEET    7  BA 7 ASN B 245  VAL B 248  1  O  ILE B 246   N  SER B 189           
SHEET    1  CA 7 LEU C  62  GLN C  64  0                                        
SHEET    2  CA 7 LYS C  34  TYR C  39  1  O  PHE C  37   N  TYR C  63           
SHEET    3  CA 7 THR C   8  MET C  12  1  O  TYR C   9   N  VAL C  36           
SHEET    4  CA 7 GLY C  89  HIS C  92  1  O  GLY C  89   N  VAL C  10           
SHEET    5  CA 7 GLY C 140  TYR C 147  1  O  SER C 141   N  VAL C  90           
SHEET    6  CA 7 ILE C 183  ALA C 190  1  O  ARG C 184   N  ILE C 142           
SHEET    7  CA 7 ASN C 245  VAL C 248  1  O  ILE C 246   N  SER C 189           
SHEET    1  DA 7 LEU D  62  GLN D  64  0                                        
SHEET    2  DA 7 LYS D  34  TYR D  39  1  O  PHE D  37   N  TYR D  63           
SHEET    3  DA 7 THR D   8  MET D  12  1  O  TYR D   9   N  VAL D  36           
SHEET    4  DA 7 GLY D  89  HIS D  92  1  O  GLY D  89   N  VAL D  10           
SHEET    5  DA 7 GLY D 140  TYR D 147  1  O  SER D 141   N  VAL D  90           
SHEET    6  DA 7 ILE D 183  ALA D 190  1  O  ARG D 184   N  ILE D 142           
SHEET    7  DA 7 ASN D 245  VAL D 248  1  O  ILE D 246   N  SER D 189           
CISPEP   1 MET A    1    LEU A    2          0        -4.66                     
SITE     1 AC1  9 ALA A  95  PHE A  96  ALA A  97  LEU A 102                    
SITE     2 AC1  9 TYR A 147  TYR A 157  MET A 160  SER A 197                    
SITE     3 AC1  9 NAP A1258                                                     
SITE     1 AC2 27 GLY A  13  ILE A  14  ALA A  15  SER A  19                    
SITE     2 AC2 27 ILE A  20  ARG A  40  LYS A  41  SER A  44                    
SITE     3 AC2 27 ILE A  65  ASP A  66  VAL A  67  SER A  93                    
SITE     4 AC2 27 ILE A  94  ALA A  95  ILE A 120  THR A 145                    
SITE     5 AC2 27 THR A 146  TYR A 147  LYS A 164  ALA A 190                    
SITE     6 AC2 27 GLY A 191  PRO A 192  ILE A 193  THR A 195                    
SITE     7 AC2 27 LEU A 196  SER A 197  TCL A1257                               
SITE     1 AC3 26 GLY B  13  ILE B  14  ALA B  15  SER B  19                    
SITE     2 AC3 26 ILE B  20  ARG B  40  LYS B  41  SER B  44                    
SITE     3 AC3 26 ILE B  65  ASP B  66  VAL B  67  SER B  93                    
SITE     4 AC3 26 ILE B  94  ALA B  95  ILE B 120  THR B 145                    
SITE     5 AC3 26 THR B 146  TYR B 147  LYS B 164  ALA B 190                    
SITE     6 AC3 26 PRO B 192  ILE B 193  THR B 195  SER B 197                    
SITE     7 AC3 26 TCL B1258  HOH B2001                                          
SITE     1 AC4  7 ALA D  97  LEU D 102  TYR D 147  TYR D 157                    
SITE     2 AC4  7 MET D 160  SER D 197  NAP D1258                               
SITE     1 AC5  7 ALA B  97  LEU B 102  TYR B 147  TYR B 157                    
SITE     2 AC5  7 MET B 160  SER B 197  NAP B1257                               
SITE     1 AC6 23 GLY C  13  ILE C  14  ALA C  15  SER C  19                    
SITE     2 AC6 23 ILE C  20  ARG C  40  LYS C  41  SER C  44                    
SITE     3 AC6 23 ILE C  65  ASP C  66  VAL C  67  SER C  93                    
SITE     4 AC6 23 ILE C  94  ALA C  95  THR C 145  THR C 146                    
SITE     5 AC6 23 TYR C 147  LYS C 164  PRO C 192  ILE C 193                    
SITE     6 AC6 23 THR C 195  SER C 197  TCL C1258                               
SITE     1 AC7  9 ALA C  97  LEU C 102  TYR C 147  TYR C 157                    
SITE     2 AC7  9 MET C 160  SER C 197  ALA C 198  VAL C 201                    
SITE     3 AC7  9 NAP C1257                                                     
SITE     1 AC8 23 GLY D  13  ILE D  14  ALA D  15  SER D  19                    
SITE     2 AC8 23 ILE D  20  ARG D  40  LYS D  41  ILE D  65                    
SITE     3 AC8 23 ASP D  66  VAL D  67  SER D  93  ILE D  94                    
SITE     4 AC8 23 ALA D  95  ILE D 120  THR D 145  THR D 146                    
SITE     5 AC8 23 TYR D 147  LYS D 164  PRO D 192  ILE D 193                    
SITE     6 AC8 23 THR D 195  SER D 197  TCL D1257                               
CRYST1   83.520  111.910  111.640  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      0.011973  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008936  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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