GenomeNet

Database: PDB
Entry: 3QJG
LinkDB: 3QJG
Original site: 3QJG 
HEADER    OXIDOREDUCTASE                          28-JAN-11   3QJG              
TITLE     EPIDERMIN BIOSYNTHESIS PROTEIN EPID FROM STAPHYLOCOCCUS AUREUS        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMIN BIOSYNTHESIS PROTEIN EPID;                       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 93062;                                               
SOURCE   4 STRAIN: SUBSP. AUREUS COL;                                           
SOURCE   5 GENE: EPID, SACOL1875;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, OXIDOREDUCTASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSIPIUK,M.MAKOWSKA-GRZYSKA,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CENTER  
AUTHOR   2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)               
REVDAT   2   08-NOV-17 3QJG    1       REMARK                                   
REVDAT   1   09-FEB-11 3QJG    0                                                
JRNL        AUTH   J.OSIPIUK,M.MAKOWSKA-GRZYSKA,K.KWON,W.F.ANDERSON,            
JRNL        AUTH 2 A.JOACHIMIAK                                                 
JRNL        TITL   EPIDERMIN BIOSYNTHESIS PROTEIN EPID FROM STAPHYLOCOCCUS      
JRNL        TITL 2 AUREUS.                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 162164                         
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8177                            
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) : 2.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8555                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 470                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16396                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 378                                     
REMARK   3   SOLVENT ATOMS            : 1504                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.66000                                              
REMARK   3    B22 (A**2) : -1.83000                                             
REMARK   3    B33 (A**2) : -3.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.65000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.215         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.194         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.445        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17744 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 11672 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24285 ; 1.629 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28924 ; 0.962 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2200 ; 6.221 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   848 ;41.908 ;25.896       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3159 ;16.314 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;18.385 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2767 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19490 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3279 ; 0.001 ; 0.020       
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): 10504 ; 0.755 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4139 ; 0.214 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17309 ; 1.289 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7240 ; 2.169 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6886 ; 3.326 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
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   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6656 119.5105  70.2432              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0564 T22:   0.0849                                     
REMARK   3      T33:   0.1033 T12:  -0.0046                                     
REMARK   3      T13:   0.0185 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7803 L22:   0.9919                                     
REMARK   3      L33:   1.0552 L12:  -0.0172                                     
REMARK   3      L13:   0.2689 L23:   0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:  -0.0225 S13:   0.0562                       
REMARK   3      S21:   0.0925 S22:   0.0056 S23:   0.0160                       
REMARK   3      S31:  -0.2096 S32:  -0.0265 S33:   0.0002                       
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   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1391  90.9091  62.4703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0890 T22:   0.0587                                     
REMARK   3      T33:   0.1129 T12:  -0.0159                                     
REMARK   3      T13:   0.0104 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4903 L22:   0.6321                                     
REMARK   3      L33:   1.2537 L12:   0.0647                                     
REMARK   3      L13:   0.0131 L23:   0.1442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0018 S12:  -0.0009 S13:  -0.0477                       
REMARK   3      S21:   0.1262 S22:   0.0085 S23:   0.0518                       
REMARK   3      S31:   0.2984 S32:  -0.0135 S33:  -0.0067                       
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   -10        C  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3647 113.4082  49.8266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0192 T22:   0.1903                                     
REMARK   3      T33:   0.1752 T12:   0.0282                                     
REMARK   3      T13:  -0.0191 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3132 L22:   1.0000                                     
REMARK   3      L33:   1.3662 L12:   0.3253                                     
REMARK   3      L13:  -0.1443 L23:  -0.1786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:   0.0175 S13:  -0.0115                       
REMARK   3      S21:  -0.0767 S22:  -0.0141 S23:   0.1728                       
REMARK   3      S31:  -0.1153 S32:  -0.2469 S33:   0.0177                       
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   -10        D  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.5356 140.6064  54.4147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1264 T22:   0.0767                                     
REMARK   3      T33:   0.0772 T12:  -0.0626                                     
REMARK   3      T13:   0.0255 T23:  -0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7179 L22:   0.9720                                     
REMARK   3      L33:   0.8350 L12:  -0.1748                                     
REMARK   3      L13:  -0.0561 L23:   0.0166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:  -0.0646 S13:  -0.0395                       
REMARK   3      S21:   0.0262 S22:   0.0588 S23:  -0.0186                       
REMARK   3      S31:  -0.2912 S32:   0.0826 S33:  -0.0508                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   -10        E  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.9699 124.4198  48.1569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0345 T22:   0.2852                                     
REMARK   3      T33:   0.2430 T12:  -0.0575                                     
REMARK   3      T13:   0.0105 T23:  -0.0788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2728 L22:   1.5948                                     
REMARK   3      L33:   1.8518 L12:   0.0286                                     
REMARK   3      L13:  -0.2733 L23:  -0.3846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0201 S12:  -0.0518 S13:  -0.0418                       
REMARK   3      S21:  -0.1136 S22:   0.0204 S23:  -0.3372                       
REMARK   3      S31:   0.0271 S32:   0.4630 S33:  -0.0406                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   -10        F  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1348 138.5507  25.8918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2154 T22:   0.1077                                     
REMARK   3      T33:   0.0550 T12:  -0.1169                                     
REMARK   3      T13:   0.0567 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7969 L22:   1.0383                                     
REMARK   3      L33:   1.1944 L12:   0.0396                                     
REMARK   3      L13:  -0.0360 L23:   0.2602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:   0.0782 S13:   0.0294                       
REMARK   3      S21:  -0.3033 S22:   0.0513 S23:  -0.0813                       
REMARK   3      S31:  -0.3437 S32:   0.1523 S33:  -0.0434                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   -10        G  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7244 100.3714   5.2951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2501 T22:   0.0492                                     
REMARK   3      T33:   0.0355 T12:  -0.0080                                     
REMARK   3      T13:   0.0001 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9143 L22:   0.6921                                     
REMARK   3      L33:   0.6962 L12:  -0.0879                                     
REMARK   3      L13:  -0.1812 L23:   0.0188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:   0.0231 S13:  -0.0853                       
REMARK   3      S21:  -0.1741 S22:  -0.0147 S23:  -0.0446                       
REMARK   3      S31:   0.1064 S32:  -0.0155 S33:   0.0272                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   -10        H  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5013 129.0184  11.3526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2563 T22:   0.0472                                     
REMARK   3      T33:   0.0565 T12:   0.0098                                     
REMARK   3      T13:  -0.0157 T23:   0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5836 L22:   0.6336                                     
REMARK   3      L33:   0.9871 L12:  -0.0048                                     
REMARK   3      L13:  -0.1276 L23:   0.2398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0679 S12:   0.0433 S13:   0.0801                       
REMARK   3      S21:  -0.1831 S22:  -0.0032 S23:  -0.0318                       
REMARK   3      S31:  -0.2830 S32:  -0.0356 S33:  -0.0647                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   -10        I  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0320 106.6044  19.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0483 T22:   0.1813                                     
REMARK   3      T33:   0.1231 T12:  -0.0264                                     
REMARK   3      T13:  -0.0634 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2466 L22:   1.7270                                     
REMARK   3      L33:   2.1781 L12:  -0.1307                                     
REMARK   3      L13:  -0.2824 L23:  -0.3771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0156 S12:   0.0202 S13:  -0.0280                       
REMARK   3      S21:  -0.0952 S22:  -0.0170 S23:   0.2555                       
REMARK   3      S31:  -0.0543 S32:  -0.3130 S33:   0.0015                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   -10        J  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.2068  79.3242  24.7710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2169 T22:   0.0573                                     
REMARK   3      T33:   0.0565 T12:   0.0515                                     
REMARK   3      T13:   0.0269 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9646 L22:   0.8704                                     
REMARK   3      L33:   0.6493 L12:   0.3029                                     
REMARK   3      L13:  -0.0007 L23:  -0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0981 S12:   0.0436 S13:   0.0162                       
REMARK   3      S21:  -0.1518 S22:   0.0677 S23:  -0.0537                       
REMARK   3      S31:   0.2763 S32:   0.0706 S33:   0.0304                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   -10        K  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.6766  81.4068  54.7751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1917 T22:   0.1038                                     
REMARK   3      T33:   0.0501 T12:   0.1108                                     
REMARK   3      T13:   0.0070 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8319 L22:   0.9935                                     
REMARK   3      L33:   1.1734 L12:  -0.0553                                     
REMARK   3      L13:   0.0330 L23:   0.3872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0603 S12:  -0.1314 S13:  -0.0013                       
REMARK   3      S21:   0.1304 S22:   0.0126 S23:  -0.0573                       
REMARK   3      S31:   0.3859 S32:   0.1178 S33:   0.0477                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   -10        L  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.4253  95.4899  36.8025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0338 T22:   0.2602                                     
REMARK   3      T33:   0.2054 T12:   0.0685                                     
REMARK   3      T13:   0.0002 T23:  -0.0660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6926 L22:   1.7177                                     
REMARK   3      L33:   1.4554 L12:  -0.0143                                     
REMARK   3      L13:  -0.0735 L23:  -0.7060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0701 S12:  -0.1144 S13:   0.0423                       
REMARK   3      S21:   0.0844 S22:   0.0723 S23:  -0.2804                       
REMARK   3      S31:   0.0069 S32:   0.3821 S33:  -0.0022                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3QJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063721.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-10                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162302                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.080                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, HKL-3000                                      
REMARK 200 STARTING MODEL: 1G5Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 20% PEG-MME-5000, PH     
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       80.49550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.62800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.49550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       55.62800            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 44140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 70510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -343.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L                                  
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    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     ASN E    -1                                                      
REMARK 465     ALA E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     ASN F    -1                                                      
REMARK 465     ALA F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     SER G    -2                                                      
REMARK 465     ASN G    -1                                                      
REMARK 465     ALA G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     SER H    -2                                                      
REMARK 465     ASN H    -1                                                      
REMARK 465     ALA H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     SER I    -2                                                      
REMARK 465     ASN I    -1                                                      
REMARK 465     ALA I     0                                                      
REMARK 465     MET I     1                                                      
REMARK 465     GLY I     2                                                      
REMARK 465     SER J    -2                                                      
REMARK 465     ASN J    -1                                                      
REMARK 465     ALA J     0                                                      
REMARK 465     MET J     1                                                      
REMARK 465     GLY J     2                                                      
REMARK 465     SER K    -2                                                      
REMARK 465     ASN K    -1                                                      
REMARK 465     ALA K     0                                                      
REMARK 465     MET K     1                                                      
REMARK 465     GLY K     2                                                      
REMARK 465     SER L    -2                                                      
REMARK 465     ASN L    -1                                                      
REMARK 465     ALA L     0                                                      
REMARK 465     MET L     1                                                      
REMARK 465     GLY L     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   OG   SER H    27     O    HOH H   857              2.05            
REMARK 500   OE2  GLU E    47     NZ   LYS E    50              2.06            
REMARK 500   OE2  GLU G    59     O    HOH G   990              2.06            
REMARK 500   OD1  ASP G    62     O    HOH G   178              2.07            
REMARK 500   OD1  ASP D    62     O    HOH D   190              2.08            
REMARK 500   O    HOH G  1122     O    HOH G  1273              2.09            
REMARK 500   OE1  GLU J    47     O    HOH J   465              2.11            
REMARK 500   OD1  ASN L    39     O    HOH L   480              2.12            
REMARK 500   O    HOH H   576     O    HOH H  1364              2.13            
REMARK 500   O    HOH K   584     O    HOH K  1305              2.14            
REMARK 500   OD1  ASP C    62     O    HOH C   173              2.14            
REMARK 500   O    HOH I   483     O    HOH I  1504              2.15            
REMARK 500   O    HOH J  1291     O    HOH J  1315              2.16            
REMARK 500   OD1  ASN G    72     NH1  ARG H   119              2.16            
REMARK 500   NZ   LYS J   167     OE1  GLU J   170              2.17            
REMARK 500   O    HOH A   336     O    HOH A  1142              2.17            
REMARK 500   OE2  GLU A    59     O    HOH A   929              2.18            
REMARK 500   NZ   LYS K   167     O    HOH K  1109              2.18            
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 B   122     O    HOH D   195     4546     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A 125   CB    VAL A 125   CG2     0.140                       
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    CYS C  95   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG E 119   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    CYS H  95   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    CYS I  95   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 106       38.65   -150.24                                   
REMARK 500    LEU B  80      121.45   -170.41                                   
REMARK 500    ALA B 106       50.51   -141.96                                   
REMARK 500    LEU C  80      115.26   -166.18                                   
REMARK 500    CYS C  95       76.65   -151.72                                   
REMARK 500    ALA C 106       44.56   -143.74                                   
REMARK 500    ALA D 106       42.17   -140.33                                   
REMARK 500    LEU E  80      111.84   -161.77                                   
REMARK 500    CYS E  95       81.39   -150.85                                   
REMARK 500    ALA E 106       50.12   -153.23                                   
REMARK 500    PRO E 142       74.10    -62.61                                   
REMARK 500    ASP F  30      -82.40    -57.55                                   
REMARK 500    ALA G 106       47.38   -149.17                                   
REMARK 500    ASN H  14       -7.71    -58.38                                   
REMARK 500    LEU H  80      119.03   -160.59                                   
REMARK 500    ALA H 106       46.77   -147.81                                   
REMARK 500    PHE I  52      -52.80   -126.52                                   
REMARK 500    CYS I  95       76.83   -152.76                                   
REMARK 500    ALA I 106       47.13   -150.60                                   
REMARK 500    ASP K  30      -72.19    -60.86                                   
REMARK 500    ALA K 106       55.07   -146.76                                   
REMARK 500    LYS L  28       -6.57   -147.74                                   
REMARK 500    ALA L 106       48.68   -147.60                                   
REMARK 500    GLU L 108      -35.23    -36.83                                   
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 FMN A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN G 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN I 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN J 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN K 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN L 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 706                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP00629   RELATED DB: TARGETDB                          
DBREF  3QJG A    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG B    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG C    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG D    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG E    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG F    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG G    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG H    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG I    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG J    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG K    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
DBREF  3QJG L    1   172  UNP    Q5HEV4   Q5HEV4_STAAC     1    172             
SEQADV 3QJG SER A   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN A   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA A    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER B   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN B   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA B    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER C   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN C   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA C    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER D   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN D   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA D    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER E   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN E   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA E    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER F   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN F   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA F    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER G   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN G   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA G    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER H   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN H   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA H    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER I   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN I   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA I    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER J   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN J   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA J    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER K   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN K   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA K    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG SER L   -2  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ASN L   -1  UNP  Q5HEV4              EXPRESSION TAG                 
SEQADV 3QJG ALA L    0  UNP  Q5HEV4              EXPRESSION TAG                 
SEQRES   1 A  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 A  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 A  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 A  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 A  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 A  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 A  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 A  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 A  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 A  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 A  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 A  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 A  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 A  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 B  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 B  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 B  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 B  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 B  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 B  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 B  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 B  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 B  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 B  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 B  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 B  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 B  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 B  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 C  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 C  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 C  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 C  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 C  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 C  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 C  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 C  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 C  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 C  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 C  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 C  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 C  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 C  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 D  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 D  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 D  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 D  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 D  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 D  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 D  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 D  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 D  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 D  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 D  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 D  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 D  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 D  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 E  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 E  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 E  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 E  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 E  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 E  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 E  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 E  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 E  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 E  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 E  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 E  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 E  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 E  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 F  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 F  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 F  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 F  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 F  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 F  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 F  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 F  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 F  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 F  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 F  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 F  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 F  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 F  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 G  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 G  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 G  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 G  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 G  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 G  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 G  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 G  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 G  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 G  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 G  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 G  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 G  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 G  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 H  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 H  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 H  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 H  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 H  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 H  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 H  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 H  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 H  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 H  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 H  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 H  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 H  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 H  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 I  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 I  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 I  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 I  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 I  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 I  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 I  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 I  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 I  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 I  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 I  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 I  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 I  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 I  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 J  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 J  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 J  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 J  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 J  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 J  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 J  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 J  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 J  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 J  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 J  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 J  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 J  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 J  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 K  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 K  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 K  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 K  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 K  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 K  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 K  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 K  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 K  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 K  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 K  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 K  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 K  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 K  175  LYS VAL LEU GLU PHE ILE                                      
SEQRES   1 L  175  SER ASN ALA MET GLY GLU ASN VAL LEU ILE CYS LEU CYS          
SEQRES   2 L  175  GLY SER VAL ASN SER ILE ASN ILE SER HIS TYR ILE ILE          
SEQRES   3 L  175  GLU LEU LYS SER LYS PHE ASP GLU VAL ASN VAL ILE ALA          
SEQRES   4 L  175  SER THR ASN GLY ARG LYS PHE ILE ASN GLY GLU ILE LEU          
SEQRES   5 L  175  LYS GLN PHE CYS ASP ASN TYR TYR ASP GLU PHE GLU ASP          
SEQRES   6 L  175  PRO PHE LEU ASN HIS VAL ASP ILE ALA ASN LYS HIS ASP          
SEQRES   7 L  175  LYS ILE ILE ILE LEU PRO ALA THR SER ASN THR ILE ASN          
SEQRES   8 L  175  LYS ILE ALA ASN GLY ILE CYS ASP ASN LEU LEU LEU THR          
SEQRES   9 L  175  ILE CYS HIS THR ALA PHE GLU LYS LEU SER ILE PHE PRO          
SEQRES  10 L  175  ASN MET ASN LEU ARG MET TRP GLU ASN PRO VAL THR GLN          
SEQRES  11 L  175  ASN ASN ILE ARG LEU LEU LYS ASP TYR GLY VAL SER ILE          
SEQRES  12 L  175  TYR PRO ALA ASN ILE SER GLU SER TYR GLU LEU ALA SER          
SEQRES  13 L  175  LYS THR PHE LYS LYS ASN VAL VAL ALA PRO GLU PRO TYR          
SEQRES  14 L  175  LYS VAL LEU GLU PHE ILE                                      
HET    FMN  A 501      31                                                       
HET     CL  A 701       1                                                       
HET     CL  A 705       1                                                       
HET    FMN  B 501      31                                                       
HET    FMN  C 501      31                                                       
HET    FMN  D 501      31                                                       
HET     CL  D 702       1                                                       
HET     CL  D 706       1                                                       
HET    FMN  E 501      31                                                       
HET    FMN  F 501      31                                                       
HET    FMN  G 501      31                                                       
HET    FMN  H 501      31                                                       
HET    FMN  I 501      31                                                       
HET    FMN  J 501      31                                                       
HET     CL  J 703       1                                                       
HET     CL  J 704       1                                                       
HET    FMN  K 501      31                                                       
HET    FMN  L 501      31                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM      CL CHLORIDE ION                                                     
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL  13  FMN    12(C17 H21 N4 O9 P)                                          
FORMUL  14   CL    6(CL 1-)                                                     
FORMUL  31  HOH   *1504(H2 O)                                                   
HELIX    1   1 SER A   12  ILE A   16  5                                   5    
HELIX    2   2 ASN A   17  LYS A   26  1                                  10    
HELIX    3   3 THR A   38  ILE A   44  5                                   7    
HELIX    4   4 ASN A   45  CYS A   53  1                                   9    
HELIX    5   5 ASN A   66  LYS A   73  1                                   8    
HELIX    6   6 THR A   83  ASN A   92  1                                  10    
HELIX    7   7 ASN A   97  THR A  105  1                                   9    
HELIX    8   8 ALA A  106  GLU A  108  5                                   3    
HELIX    9   9 LEU A  118  GLU A  122  1                                   5    
HELIX   10  10 ASN A  123  TYR A  136  1                                  14    
HELIX   11  11 GLU A  164  ILE A  172  1                                   9    
HELIX   12  12 SER B   12  ILE B   16  5                                   5    
HELIX   13  13 ASN B   17  LYS B   26  1                                  10    
HELIX   14  14 GLY B   40  ILE B   44  5                                   5    
HELIX   15  15 ASN B   45  GLN B   51  1                                   7    
HELIX   16  16 ASN B   66  LYS B   73  1                                   8    
HELIX   17  17 THR B   83  ASN B   92  1                                  10    
HELIX   18  18 ASN B   97  ALA B  106  1                                  10    
HELIX   19  19 LEU B  118  GLU B  122  1                                   5    
HELIX   20  20 ASN B  123  TYR B  136  1                                  14    
HELIX   21  21 GLU B  164  ILE B  172  1                                   9    
HELIX   22  22 SER C   12  ILE C   16  5                                   5    
HELIX   23  23 ASN C   17  PHE C   29  1                                  13    
HELIX   24  24 THR C   38  ILE C   44  5                                   7    
HELIX   25  25 ASN C   45  LYS C   50  1                                   6    
HELIX   26  26 ASN C   66  HIS C   74  1                                   9    
HELIX   27  27 THR C   83  ASN C   92  1                                  10    
HELIX   28  28 ASN C   97  THR C  105  1                                   9    
HELIX   29  29 ALA C  106  GLU C  108  5                                   3    
HELIX   30  30 LEU C  118  GLU C  122  1                                   5    
HELIX   31  31 ASN C  123  TYR C  136  1                                  14    
HELIX   32  32 GLU C  164  ILE C  172  1                                   9    
HELIX   33  33 SER D   12  ILE D   16  5                                   5    
HELIX   34  34 ASN D   17  LYS D   26  1                                  10    
HELIX   35  35 THR D   38  ILE D   44  5                                   7    
HELIX   36  36 ASN D   45  LYS D   50  1                                   6    
HELIX   37  37 ASN D   66  LYS D   73  1                                   8    
HELIX   38  38 THR D   83  ASN D   92  1                                  10    
HELIX   39  39 ASN D   97  ALA D  106  1                                  10    
HELIX   40  40 LEU D  118  GLU D  122  1                                   5    
HELIX   41  41 ASN D  123  TYR D  136  1                                  14    
HELIX   42  42 GLU D  164  ILE D  172  1                                   9    
HELIX   43  43 SER E   12  ILE E   16  5                                   5    
HELIX   44  44 ASN E   17  SER E   27  1                                  11    
HELIX   45  45 THR E   38  ILE E   44  5                                   7    
HELIX   46  46 ASN E   45  GLN E   51  1                                   7    
HELIX   47  47 ASN E   66  LYS E   73  1                                   8    
HELIX   48  48 THR E   83  ALA E   91  1                                   9    
HELIX   49  49 ASN E   97  THR E  105  1                                   9    
HELIX   50  50 ALA E  106  GLU E  108  5                                   3    
HELIX   51  51 LEU E  118  GLU E  122  1                                   5    
HELIX   52  52 ASN E  123  TYR E  136  1                                  14    
HELIX   53  53 GLU E  164  ILE E  172  1                                   9    
HELIX   54  54 SER F   12  ILE F   16  5                                   5    
HELIX   55  55 ASN F   17  LYS F   26  1                                  10    
HELIX   56  56 GLY F   40  ILE F   44  5                                   5    
HELIX   57  57 ASN F   45  CYS F   53  1                                   9    
HELIX   58  58 ASN F   66  HIS F   74  1                                   9    
HELIX   59  59 THR F   83  ASN F   92  1                                  10    
HELIX   60  60 ASN F   97  THR F  105  1                                   9    
HELIX   61  61 ALA F  106  GLU F  108  5                                   3    
HELIX   62  62 LEU F  118  GLU F  122  1                                   5    
HELIX   63  63 ASN F  123  TYR F  136  1                                  14    
HELIX   64  64 GLU F  164  ILE F  172  1                                   9    
HELIX   65  65 SER G   12  ILE G   16  5                                   5    
HELIX   66  66 ASN G   17  LYS G   26  1                                  10    
HELIX   67  67 THR G   38  ILE G   44  5                                   7    
HELIX   68  68 ASN G   45  CYS G   53  1                                   9    
HELIX   69  69 ASN G   66  LYS G   73  1                                   8    
HELIX   70  70 THR G   83  ASN G   92  1                                  10    
HELIX   71  71 ASN G   97  ALA G  106  1                                  10    
HELIX   72  72 LEU G  118  GLU G  122  1                                   5    
HELIX   73  73 ASN G  123  TYR G  136  1                                  14    
HELIX   74  74 GLU G  164  ILE G  172  1                                   9    
HELIX   75  75 SER H   12  ILE H   16  5                                   5    
HELIX   76  76 ASN H   17  LYS H   26  1                                  10    
HELIX   77  77 GLY H   40  ILE H   44  5                                   5    
HELIX   78  78 ASN H   45  GLN H   51  1                                   7    
HELIX   79  79 ASN H   66  HIS H   74  1                                   9    
HELIX   80  80 THR H   83  GLY H   93  1                                  11    
HELIX   81  81 ASN H   97  THR H  105  1                                   9    
HELIX   82  82 ALA H  106  GLU H  108  5                                   3    
HELIX   83  83 LEU H  118  GLU H  122  1                                   5    
HELIX   84  84 ASN H  123  TYR H  136  1                                  14    
HELIX   85  85 GLU H  164  ILE H  172  1                                   9    
HELIX   86  86 SER I   12  ILE I   16  5                                   5    
HELIX   87  87 ASN I   17  LYS I   26  1                                  10    
HELIX   88  88 THR I   38  ILE I   44  5                                   7    
HELIX   89  89 ASN I   45  LYS I   50  1                                   6    
HELIX   90  90 ASN I   66  LYS I   73  1                                   8    
HELIX   91  91 THR I   83  ASN I   92  1                                  10    
HELIX   92  92 ASN I   97  THR I  105  1                                   9    
HELIX   93  93 ALA I  106  GLU I  108  5                                   3    
HELIX   94  94 LEU I  118  GLU I  122  1                                   5    
HELIX   95  95 ASN I  123  TYR I  136  1                                  14    
HELIX   96  96 GLU I  164  ILE I  172  1                                   9    
HELIX   97  97 SER J   12  ILE J   16  5                                   5    
HELIX   98  98 ASN J   17  LYS J   26  1                                  10    
HELIX   99  99 THR J   38  ILE J   44  5                                   7    
HELIX  100 100 ASN J   45  LYS J   50  1                                   6    
HELIX  101 101 ASN J   66  LYS J   73  1                                   8    
HELIX  102 102 THR J   83  ASN J   92  1                                  10    
HELIX  103 103 ASN J   97  ALA J  106  1                                  10    
HELIX  104 104 LEU J  118  GLU J  122  1                                   5    
HELIX  105 105 ASN J  123  TYR J  136  1                                  14    
HELIX  106 106 GLU J  164  ILE J  172  1                                   9    
HELIX  107 107 SER K   12  ILE K   16  5                                   5    
HELIX  108 108 ASN K   17  LYS K   26  1                                  10    
HELIX  109 109 GLY K   40  ILE K   44  5                                   5    
HELIX  110 110 ASN K   45  GLN K   51  1                                   7    
HELIX  111 111 ASN K   66  HIS K   74  1                                   9    
HELIX  112 112 THR K   83  ASN K   92  1                                  10    
HELIX  113 113 ASN K   97  ALA K  106  1                                  10    
HELIX  114 114 LEU K  118  GLU K  122  1                                   5    
HELIX  115 115 ASN K  123  TYR K  136  1                                  14    
HELIX  116 116 GLU K  164  ILE K  172  1                                   9    
HELIX  117 117 SER L   12  ILE L   16  5                                   5    
HELIX  118 118 ASN L   17  LYS L   26  1                                  10    
HELIX  119 119 GLY L   40  ILE L   44  5                                   5    
HELIX  120 120 ASN L   45  LYS L   50  1                                   6    
HELIX  121 121 ASN L   66  LYS L   73  1                                   8    
HELIX  122 122 THR L   83  GLY L   93  1                                  11    
HELIX  123 123 ASN L   97  THR L  105  1                                   9    
HELIX  124 124 ALA L  106  GLU L  108  5                                   3    
HELIX  125 125 LEU L  118  GLU L  122  1                                   5    
HELIX  126 126 ASN L  123  TYR L  136  1                                  14    
HELIX  127 127 GLU L  164  ILE L  172  1                                   9    
SHEET    1   A 6 TYR A  56  TYR A  57  0                                        
SHEET    2   A 6 GLU A  31  ALA A  36  1  N  VAL A  34   O  TYR A  57           
SHEET    3   A 6 ASN A   4  LEU A   9  1  N  ILE A   7   O  ASN A  33           
SHEET    4   A 6 LYS A  76  ALA A  82  1  O  ILE A  78   N  CYS A   8           
SHEET    5   A 6 LEU A 110  PRO A 114  1  O  SER A 111   N  ILE A  79           
SHEET    6   A 6 SER A 139  ILE A 140  1  O  SER A 139   N  ILE A 112           
SHEET    1   B 3 MET A 116  ASN A 117  0                                        
SHEET    2   B 3 THR A 155  VAL A 160 -1  O  VAL A 160   N  MET A 116           
SHEET    3   B 3 ILE A 145  GLU A 150 -1  N  GLU A 150   O  THR A 155           
SHEET    1   C 6 TYR B  56  TYR B  57  0                                        
SHEET    2   C 6 VAL B  32  ALA B  36  1  N  VAL B  34   O  TYR B  57           
SHEET    3   C 6 VAL B   5  LEU B   9  1  N  LEU B   9   O  ILE B  35           
SHEET    4   C 6 LYS B  76  ALA B  82  1  O  ILE B  78   N  LEU B   6           
SHEET    5   C 6 LEU B 110  PRO B 114  1  O  SER B 111   N  ILE B  79           
SHEET    6   C 6 SER B 139  ILE B 140  1  O  SER B 139   N  ILE B 112           
SHEET    1   D 3 MET B 116  ASN B 117  0                                        
SHEET    2   D 3 THR B 155  VAL B 160 -1  O  VAL B 160   N  MET B 116           
SHEET    3   D 3 ILE B 145  GLU B 150 -1  N  SER B 148   O  LYS B 157           
SHEET    1   E 6 TYR C  56  TYR C  57  0                                        
SHEET    2   E 6 VAL C  32  ALA C  36  1  N  VAL C  34   O  TYR C  57           
SHEET    3   E 6 VAL C   5  LEU C   9  1  N  LEU C   9   O  ILE C  35           
SHEET    4   E 6 LYS C  76  ALA C  82  1  O  ILE C  78   N  CYS C   8           
SHEET    5   E 6 LEU C 110  PRO C 114  1  O  PHE C 113   N  ALA C  82           
SHEET    6   E 6 SER C 139  ILE C 140  1  O  SER C 139   N  ILE C 112           
SHEET    1   F 3 MET C 116  ASN C 117  0                                        
SHEET    2   F 3 THR C 155  VAL C 160 -1  O  VAL C 160   N  MET C 116           
SHEET    3   F 3 ILE C 145  GLU C 150 -1  N  SER C 148   O  LYS C 157           
SHEET    1   G 6 TYR D  56  TYR D  57  0                                        
SHEET    2   G 6 GLU D  31  ALA D  36  1  N  VAL D  34   O  TYR D  57           
SHEET    3   G 6 ASN D   4  LEU D   9  1  N  ILE D   7   O  ASN D  33           
SHEET    4   G 6 LYS D  76  ALA D  82  1  O  ILE D  78   N  LEU D   6           
SHEET    5   G 6 LEU D 110  PRO D 114  1  O  SER D 111   N  ILE D  79           
SHEET    6   G 6 SER D 139  ILE D 140  1  O  SER D 139   N  ILE D 112           
SHEET    1   H 3 MET D 116  ASN D 117  0                                        
SHEET    2   H 3 THR D 155  VAL D 160 -1  O  VAL D 160   N  MET D 116           
SHEET    3   H 3 ILE D 145  GLU D 150 -1  N  GLU D 150   O  THR D 155           
SHEET    1   I 6 TYR E  56  TYR E  57  0                                        
SHEET    2   I 6 GLU E  31  ALA E  36  1  N  VAL E  34   O  TYR E  57           
SHEET    3   I 6 ASN E   4  LEU E   9  1  N  LEU E   9   O  ILE E  35           
SHEET    4   I 6 LYS E  76  ALA E  82  1  O  ILE E  78   N  CYS E   8           
SHEET    5   I 6 LEU E 110  PRO E 114  1  O  PHE E 113   N  ILE E  79           
SHEET    6   I 6 SER E 139  ILE E 140  1  O  SER E 139   N  ILE E 112           
SHEET    1   J 3 MET E 116  ASN E 117  0                                        
SHEET    2   J 3 THR E 155  VAL E 160 -1  O  VAL E 160   N  MET E 116           
SHEET    3   J 3 ILE E 145  GLU E 150 -1  N  SER E 146   O  ASN E 159           
SHEET    1   K 6 TYR F  56  TYR F  57  0                                        
SHEET    2   K 6 VAL F  32  ALA F  36  1  N  VAL F  34   O  TYR F  57           
SHEET    3   K 6 VAL F   5  LEU F   9  1  N  ILE F   7   O  ASN F  33           
SHEET    4   K 6 LYS F  76  ALA F  82  1  O  ILE F  78   N  CYS F   8           
SHEET    5   K 6 LEU F 110  PRO F 114  1  O  PHE F 113   N  ILE F  79           
SHEET    6   K 6 SER F 139  ILE F 140  1  O  SER F 139   N  ILE F 112           
SHEET    1   L 3 MET F 116  ASN F 117  0                                        
SHEET    2   L 3 THR F 155  VAL F 160 -1  O  VAL F 160   N  MET F 116           
SHEET    3   L 3 ILE F 145  GLU F 150 -1  N  SER F 146   O  ASN F 159           
SHEET    1   M 6 ASN G  55  TYR G  57  0                                        
SHEET    2   M 6 VAL G  32  ALA G  36  1  N  VAL G  34   O  TYR G  57           
SHEET    3   M 6 VAL G   5  LEU G   9  1  N  ILE G   7   O  ASN G  33           
SHEET    4   M 6 LYS G  76  ALA G  82  1  O  ILE G  78   N  LEU G   6           
SHEET    5   M 6 LEU G 110  PRO G 114  1  O  PHE G 113   N  ILE G  79           
SHEET    6   M 6 SER G 139  ILE G 140  1  O  SER G 139   N  ILE G 112           
SHEET    1   N 3 MET G 116  ASN G 117  0                                        
SHEET    2   N 3 THR G 155  VAL G 160 -1  O  VAL G 160   N  MET G 116           
SHEET    3   N 3 ILE G 145  GLU G 150 -1  N  GLU G 150   O  THR G 155           
SHEET    1   O 6 TYR H  56  TYR H  57  0                                        
SHEET    2   O 6 VAL H  32  ALA H  36  1  N  VAL H  34   O  TYR H  57           
SHEET    3   O 6 VAL H   5  LEU H   9  1  N  ILE H   7   O  ASN H  33           
SHEET    4   O 6 LYS H  76  ALA H  82  1  O  ILE H  78   N  LEU H   6           
SHEET    5   O 6 LEU H 110  PRO H 114  1  O  SER H 111   N  ILE H  79           
SHEET    6   O 6 SER H 139  ILE H 140  1  O  SER H 139   N  ILE H 112           
SHEET    1   P 3 MET H 116  ASN H 117  0                                        
SHEET    2   P 3 THR H 155  VAL H 160 -1  O  VAL H 160   N  MET H 116           
SHEET    3   P 3 ILE H 145  GLU H 150 -1  N  GLU H 150   O  THR H 155           
SHEET    1   Q 6 TYR I  56  TYR I  57  0                                        
SHEET    2   Q 6 VAL I  32  ALA I  36  1  N  VAL I  34   O  TYR I  57           
SHEET    3   Q 6 VAL I   5  LEU I   9  1  N  LEU I   9   O  ILE I  35           
SHEET    4   Q 6 LYS I  76  ALA I  82  1  O  ILE I  78   N  CYS I   8           
SHEET    5   Q 6 LEU I 110  PRO I 114  1  O  PHE I 113   N  ALA I  82           
SHEET    6   Q 6 SER I 139  ILE I 140  1  O  SER I 139   N  ILE I 112           
SHEET    1   R 3 MET I 116  ASN I 117  0                                        
SHEET    2   R 3 THR I 155  VAL I 160 -1  O  VAL I 160   N  MET I 116           
SHEET    3   R 3 ILE I 145  GLU I 150 -1  N  GLU I 150   O  THR I 155           
SHEET    1   S 6 TYR J  56  TYR J  57  0                                        
SHEET    2   S 6 VAL J  32  ALA J  36  1  N  VAL J  34   O  TYR J  57           
SHEET    3   S 6 VAL J   5  LEU J   9  1  N  ILE J   7   O  ASN J  33           
SHEET    4   S 6 LYS J  76  ALA J  82  1  O  ILE J  78   N  CYS J   8           
SHEET    5   S 6 LEU J 110  PRO J 114  1  O  PHE J 113   N  ILE J  79           
SHEET    6   S 6 SER J 139  ILE J 140  1  O  SER J 139   N  ILE J 112           
SHEET    1   T 3 MET J 116  ASN J 117  0                                        
SHEET    2   T 3 THR J 155  VAL J 160 -1  O  VAL J 160   N  MET J 116           
SHEET    3   T 3 ILE J 145  GLU J 150 -1  N  GLU J 150   O  THR J 155           
SHEET    1   U 6 TYR K  56  TYR K  57  0                                        
SHEET    2   U 6 VAL K  32  ALA K  36  1  N  VAL K  34   O  TYR K  57           
SHEET    3   U 6 VAL K   5  LEU K   9  1  N  LEU K   9   O  ILE K  35           
SHEET    4   U 6 LYS K  76  ALA K  82  1  O  ILE K  78   N  CYS K   8           
SHEET    5   U 6 LEU K 110  PRO K 114  1  O  PHE K 113   N  ILE K  79           
SHEET    6   U 6 SER K 139  ILE K 140  1  O  SER K 139   N  ILE K 112           
SHEET    1   V 3 MET K 116  ASN K 117  0                                        
SHEET    2   V 3 THR K 155  VAL K 160 -1  O  VAL K 160   N  MET K 116           
SHEET    3   V 3 ILE K 145  GLU K 150 -1  N  SER K 146   O  ASN K 159           
SHEET    1   W 6 TYR L  56  TYR L  57  0                                        
SHEET    2   W 6 GLU L  31  ALA L  36  1  N  VAL L  34   O  TYR L  57           
SHEET    3   W 6 ASN L   4  LEU L   9  1  N  VAL L   5   O  ASN L  33           
SHEET    4   W 6 LYS L  76  ALA L  82  1  O  ILE L  78   N  LEU L   6           
SHEET    5   W 6 LEU L 110  PRO L 114  1  O  PHE L 113   N  ALA L  82           
SHEET    6   W 6 SER L 139  ILE L 140  1  O  SER L 139   N  ILE L 112           
SHEET    1   X 3 MET L 116  ASN L 117  0                                        
SHEET    2   X 3 THR L 155  VAL L 160 -1  O  VAL L 160   N  MET L 116           
SHEET    3   X 3 ILE L 145  GLU L 150 -1  N  GLU L 150   O  THR L 155           
CISPEP   1 LEU A   80    PRO A   81          0        -9.84                     
CISPEP   2 LEU B   80    PRO B   81          0       -10.66                     
CISPEP   3 LEU C   80    PRO C   81          0        -5.43                     
CISPEP   4 LEU D   80    PRO D   81          0        -6.04                     
CISPEP   5 LEU E   80    PRO E   81          0        -2.96                     
CISPEP   6 LEU F   80    PRO F   81          0       -13.76                     
CISPEP   7 LEU G   80    PRO G   81          0       -10.41                     
CISPEP   8 LEU H   80    PRO H   81          0        -8.68                     
CISPEP   9 LEU I   80    PRO I   81          0        -7.04                     
CISPEP  10 LEU J   80    PRO J   81          0        -8.20                     
CISPEP  11 LEU K   80    PRO K   81          0       -12.28                     
CISPEP  12 LEU L   80    PRO L   81          0        -4.37                     
SITE     1 AC1 25 GLY A  11  SER A  12  SER A  37  ASN A  39                    
SITE     2 AC1 25 PHE A  43  THR A  83  SER A  84  ASN A  85                    
SITE     3 AC1 25 THR A  86  ASN A 115  MET A 116  HOH A 174                    
SITE     4 AC1 25 HOH A 175  HOH A 178  HOH A 290  HOH A 504                    
SITE     5 AC1 25 HOH A 511  HOH A 565   CL A 705  HOH A 773                    
SITE     6 AC1 25 LEU C  65  HIS C  67  CYS C  95  ASP C  96                    
SITE     7 AC1 25 THR C 101                                                     
SITE     1 AC2 27 PHE A  64  LEU A  65  HIS A  67  CYS A  95                    
SITE     2 AC2 27 ASP A  96  THR A 101   CL A 701  CYS B  10                    
SITE     3 AC2 27 GLY B  11  SER B  12  SER B  37  ASN B  39                    
SITE     4 AC2 27 THR B  83  SER B  84  ASN B  85  THR B  86                    
SITE     5 AC2 27 ASN B 115  MET B 116  MET B 120  HOH B 174                    
SITE     6 AC2 27 HOH B 176  HOH B 177  HOH B 215  HOH B 357                    
SITE     7 AC2 27 HOH B 640  HOH B 742  HOH B 927                               
SITE     1 AC3 28 PRO B  63  PHE B  64  LEU B  65  HIS B  67                    
SITE     2 AC3 28 CYS B  95  ASP B  96  THR B 101  CYS C  10                    
SITE     3 AC3 28 GLY C  11  SER C  12  VAL C  13  SER C  37                    
SITE     4 AC3 28 ASN C  39  PHE C  43  THR C  83  SER C  84                    
SITE     5 AC3 28 ASN C  85  THR C  86  ASN C 115  MET C 116                    
SITE     6 AC3 28 MET C 120  HOH C 175  HOH C 184  HOH C 253                    
SITE     7 AC3 28 HOH C 389  HOH C 446  HOH C 486  HOH C 611                    
SITE     1 AC4 27 CYS D  10  GLY D  11  SER D  12  SER D  37                    
SITE     2 AC4 27 ASN D  39  PHE D  43  THR D  83  SER D  84                    
SITE     3 AC4 27 ASN D  85  THR D  86  ASN D 115  MET D 116                    
SITE     4 AC4 27 MET D 120  HOH D 174  HOH D 178  HOH D 194                    
SITE     5 AC4 27 HOH D 295  HOH D 383  HOH D 405  HOH D 635                    
SITE     6 AC4 27  CL D 706  HOH D1279  LEU E  65  HIS E  67                    
SITE     7 AC4 27 CYS E  95  ASP E  96  THR E 101                               
SITE     1 AC5 24 CYS E  10  GLY E  11  SER E  12  SER E  37                    
SITE     2 AC5 24 ASN E  39  THR E  83  SER E  84  ASN E  85                    
SITE     3 AC5 24 THR E  86  ASN E 115  MET E 116  HOH E 174                    
SITE     4 AC5 24 HOH E 298  HOH E 324  HOH E 334  HOH E 644                    
SITE     5 AC5 24 HOH E 856  HOH E1272  PHE F  64  LEU F  65                    
SITE     6 AC5 24 HIS F  67  CYS F  95  ASP F  96  THR F 101                    
SITE     1 AC6 26 PHE D  64  LEU D  65  HIS D  67  CYS D  95                    
SITE     2 AC6 26 ASP D  96  THR D 101   CL D 702  CYS F  10                    
SITE     3 AC6 26 GLY F  11  SER F  12  VAL F  13  SER F  37                    
SITE     4 AC6 26 ASN F  39  THR F  83  SER F  84  ASN F  85                    
SITE     5 AC6 26 THR F  86  ASN F 115  MET F 116  MET F 120                    
SITE     6 AC6 26 HOH F 180  HOH F 211  HOH F 438  HOH F 566                    
SITE     7 AC6 26 HOH F 567  HOH F 598                                          
SITE     1 AC7 27 CYS G  10  GLY G  11  SER G  12  SER G  37                    
SITE     2 AC7 27 ASN G  39  PHE G  43  THR G  83  SER G  84                    
SITE     3 AC7 27 ASN G  85  THR G  86  ASN G 115  MET G 116                    
SITE     4 AC7 27 MET G 120  HOH G 184  HOH G 188  HOH G 189                    
SITE     5 AC7 27 HOH G 191  HOH G 270  HOH G 287  HOH G 626                    
SITE     6 AC7 27 HOH G 829  PHE I  64  LEU I  65  HIS I  67                    
SITE     7 AC7 27 CYS I  95  ASP I  96  THR I 101                               
SITE     1 AC8 25 PHE G  64  LEU G  65  HIS G  67  CYS G  95                    
SITE     2 AC8 25 ASP G  96  THR G 101  CYS H  10  GLY H  11                    
SITE     3 AC8 25 SER H  12  SER H  37  ASN H  39  THR H  83                    
SITE     4 AC8 25 SER H  84  ASN H  85  THR H  86  ASN H 115                    
SITE     5 AC8 25 MET H 116  MET H 120  HOH H 173  HOH H 176                    
SITE     6 AC8 25 HOH H 180  HOH H 210  HOH H 288  HOH H 666                    
SITE     7 AC8 25 HOH H 768                                                     
SITE     1 AC9 27 PHE H  64  LEU H  65  HIS H  67  CYS H  95                    
SITE     2 AC9 27 ASP H  96  THR H 101  CYS I  10  GLY I  11                    
SITE     3 AC9 27 SER I  12  SER I  37  ASN I  39  PHE I  43                    
SITE     4 AC9 27 THR I  83  SER I  84  ASN I  85  THR I  86                    
SITE     5 AC9 27 ASN I 115  MET I 116  MET I 120  HOH I 176                    
SITE     6 AC9 27 HOH I 177  HOH I 178  HOH I 213  HOH I 387                    
SITE     7 AC9 27 HOH I 622  HOH I 677  HOH I1262                               
SITE     1 BC1 27 CYS J  10  GLY J  11  SER J  12  VAL J  13                    
SITE     2 BC1 27 SER J  37  ASN J  39  PHE J  43  THR J  83                    
SITE     3 BC1 27 SER J  84  ASN J  85  THR J  86  ASN J 115                    
SITE     4 BC1 27 MET J 116  MET J 120  HOH J 177  HOH J 187                    
SITE     5 BC1 27 HOH J 245  HOH J 308  HOH J 492  HOH J 553                    
SITE     6 BC1 27  CL J 704  HOH J 731  LEU L  65  HIS L  67                    
SITE     7 BC1 27 CYS L  95  ASP L  96  THR L 101                               
SITE     1 BC2 28 LEU J  65  HIS J  67  CYS J  95  ASP J  96                    
SITE     2 BC2 28 THR J 101   CL J 703  CYS K  10  GLY K  11                    
SITE     3 BC2 28 SER K  12  VAL K  13  SER K  37  ASN K  39                    
SITE     4 BC2 28 PHE K  43  THR K  83  SER K  84  ASN K  85                    
SITE     5 BC2 28 THR K  86  ASN K 115  MET K 116  MET K 120                    
SITE     6 BC2 28 HOH K 175  HOH K 176  HOH K 179  HOH K 187                    
SITE     7 BC2 28 HOH K 320  HOH K 338  HOH K 452  HOH K 709                    
SITE     1 BC3 25 LEU K  65  HIS K  67  CYS K  95  ASP K  96                    
SITE     2 BC3 25 THR K 101  CYS L  10  GLY L  11  SER L  12                    
SITE     3 BC3 25 VAL L  13  SER L  37  ASN L  39  THR L  83                    
SITE     4 BC3 25 SER L  84  ASN L  85  THR L  86  ASN L 115                    
SITE     5 BC3 25 MET L 116  MET L 120  HOH L 183  HOH L 184                    
SITE     6 BC3 25 HOH L 193  HOH L 750  HOH L 753  HOH L1001                    
SITE     7 BC3 25 HOH L1455                                                     
SITE     1 BC4  5 HIS A  67  ASN B 117  HOH B 303  FMN B 501                    
SITE     2 BC4  5 HOH B 927                                                     
SITE     1 BC5  4 HIS D  67  HOH D 252  ASN F 117  FMN F 501                    
SITE     1 BC6  4 HIS J  67  ASN K 117  HOH K 386  FMN K 501                    
SITE     1 BC7  3 ASN J 117  FMN J 501  HIS L  67                               
SITE     1 BC8  4 ASN A 117  FMN A 501  HOH A 511  HIS C  67                    
SITE     1 BC9  5 ASN D 117  MET D 120  HOH D 383  FMN D 501                    
SITE     2 BC9  5 HIS E  67                                                     
CRYST1  160.991  111.256  154.569  90.00  97.25  90.00 C 1 2 1      48          
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      0.006212  0.000000  0.000790        0.00000                         
SCALE2      0.000000  0.008988  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006522        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system