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Database: PDB
Entry: 3FFL
LinkDB: 3FFL
Original site: 3FFL 
HEADER    CELL CYCLE                              03-DEC-08   3FFL              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF ANAPHASE-PROMOTING      
TITLE    2 COMPLEX SUBUNIT 7                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANAPHASE-PROMOTING COMPLEX SUBUNIT 7;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN;                                         
COMPND   5 SYNONYM: APC7, CYCLOSOME SUBUNIT 7;                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ANAPC7, APC7;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    TETRATRICOPEPTIDE REPEAT MOTIF, HELIS-TURN-HELIX, CELL CYCLE, CELL    
KEYWDS   2 DIVISION, MITOSIS, TPR REPEAT, UBL CONJUGATION PATHWAY               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.HAN,K.KIM,Y.KIM,Y.KIM                                               
REVDAT   2   11-APR-12 3FFL    1       REMARK VERSN                             
REVDAT   1   16-DEC-08 3FFL    0                                                
JRNL        AUTH   D.HAN,K.KIM,Y.KIM,Y.KANG,Y.KIM                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF                
JRNL        TITL 2 ANAPHASE-PROMOTING COMPLEX SUBUNIT 7                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 24411                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1300                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1214                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.4500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3997                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.25000                                              
REMARK   3    B22 (A**2) : -0.82000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.08000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.386         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.235         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.890        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4065 ; 0.004 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5493 ; 0.822 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   492 ; 4.134 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;35.707 ;24.773       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   769 ;17.204 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;19.970 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   640 ; 0.050 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2956 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2508 ; 0.183 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4048 ; 0.359 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1557 ; 0.528 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1445 ; 0.893 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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    21        A    74                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4260  -0.5930 -38.2980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5619 T22:   0.3687                                     
REMARK   3      T33:   0.1244 T12:   0.0340                                     
REMARK   3      T13:  -0.0837 T23:  -0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0892 L22:   5.1289                                     
REMARK   3      L33:  14.5493 L12:  -0.5291                                     
REMARK   3      L13:   3.1779 L23:   2.6311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2638 S12:   0.4809 S13:  -0.4342                       
REMARK   3      S21:  -0.9052 S22:   0.1139 S23:  -0.1513                       
REMARK   3      S31:   0.5655 S32:   0.0455 S33:  -0.3778                       
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 :   A    75        A   133                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4700   4.2630 -25.4530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2575 T22:   0.3511                                     
REMARK   3      T33:   0.1018 T12:  -0.0186                                     
REMARK   3      T13:  -0.0397 T23:   0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7673 L22:   8.6588                                     
REMARK   3      L33:  15.3182 L12:   0.4244                                     
REMARK   3      L13:   2.9080 L23:   3.6650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1909 S12:   0.0230 S13:   0.0016                       
REMARK   3      S21:  -0.7621 S22:  -0.0303 S23:  -0.1112                       
REMARK   3      S31:   0.1798 S32:  -0.2724 S33:  -0.1606                       
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 :   A   134        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2920  11.5490 -15.0660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1987 T22:   0.3487                                     
REMARK   3      T33:   0.1494 T12:   0.0007                                     
REMARK   3      T13:  -0.0053 T23:  -0.0505                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7949 L22:   4.7881                                     
REMARK   3      L33:  13.3654 L12:   1.6663                                     
REMARK   3      L13:   3.5339 L23:   2.0999                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0531 S12:  -0.5328 S13:   0.4283                       
REMARK   3      S21:  -0.3747 S22:  -0.0270 S23:  -0.1171                       
REMARK   3      S31:  -0.9826 S32:  -0.0230 S33:   0.0801                       
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 :   B    21        B    72                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6410  -1.9010   2.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0503 T22:   0.7369                                     
REMARK   3      T33:   0.5725 T12:   0.0293                                     
REMARK   3      T13:  -0.2359 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9284 L22:   8.9670                                     
REMARK   3      L33:   5.3574 L12:  -2.1781                                     
REMARK   3      L13:  -0.9996 L23:   2.4361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2370 S12:  -0.5814 S13:  -0.2490                       
REMARK   3      S21:   0.7503 S22:   0.4238 S23:  -1.5727                       
REMARK   3      S31:   0.4568 S32:   0.5028 S33:  -0.1868                       
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 :   B    73        B   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0410   3.6110   2.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0150 T22:   0.5908                                     
REMARK   3      T33:   0.1312 T12:  -0.0341                                     
REMARK   3      T13:  -0.1230 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3939 L22:   4.1711                                     
REMARK   3      L33:   8.6141 L12:  -1.6489                                     
REMARK   3      L13:   0.2291 L23:  -0.1166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0863 S12:  -0.6752 S13:  -0.1989                       
REMARK   3      S21:   0.3193 S22:   0.0862 S23:  -0.5470                       
REMARK   3      S31:  -0.0839 S32:   0.0561 S33:   0.0001                       
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 :   B   137        B   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5920  10.7140   9.1650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1359 T22:   0.6088                                     
REMARK   3      T33:   0.1201 T12:  -0.0074                                     
REMARK   3      T13:  -0.0556 T23:  -0.1267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9473 L22:   5.9409                                     
REMARK   3      L33:  10.0423 L12:   0.7243                                     
REMARK   3      L13:   2.1216 L23:   1.7215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:  -0.5985 S13:   0.5664                       
REMARK   3      S21:   0.3702 S22:   0.0335 S23:  -0.0962                       
REMARK   3      S31:  -0.7379 S32:   0.0720 S33:  -0.0648                       
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 :   C    22        C    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5810  33.2030 -29.3890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4627 T22:   0.6427                                     
REMARK   3      T33:   0.1304 T12:  -0.0191                                     
REMARK   3      T13:   0.0127 T23:   0.0918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1635 L22:   4.5960                                     
REMARK   3      L33:  11.4348 L12:   0.6563                                     
REMARK   3      L13:   2.8768 L23:   0.4996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0229 S12:   0.6737 S13:  -0.0295                       
REMARK   3      S21:  -1.1156 S22:   0.1506 S23:  -0.1303                       
REMARK   3      S31:   0.0940 S32:   0.7998 S33:  -0.1735                       
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 :   C    69        C   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5440  34.0590 -17.3520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1976 T22:   0.5192                                     
REMARK   3      T33:   0.0994 T12:  -0.0396                                     
REMARK   3      T13:   0.0033 T23:   0.1062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1709 L22:   7.4134                                     
REMARK   3      L33:  10.7104 L12:  -1.3262                                     
REMARK   3      L13:   2.2724 L23:   1.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1157 S12:   0.3462 S13:   0.0358                       
REMARK   3      S21:  -0.5923 S22:  -0.0193 S23:  -0.3643                       
REMARK   3      S31:   0.1433 S32:   0.6497 S33:  -0.0964                       
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 :   C   125        C   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3500  38.7080  -4.6120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1131 T22:   0.6449                                     
REMARK   3      T33:   0.2293 T12:  -0.0491                                     
REMARK   3      T13:  -0.0458 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8173 L22:   4.8762                                     
REMARK   3      L33:   8.1403 L12:   0.4213                                     
REMARK   3      L13:   2.9751 L23:   0.9138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1981 S12:  -0.2859 S13:   0.5391                       
REMARK   3      S21:   0.0058 S22:   0.0888 S23:  -0.3152                       
REMARK   3      S31:  -0.3757 S32:   0.4281 S33:   0.1093                       
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 :   D    22        D    41                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0690  30.4770   8.4180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2055 T22:   0.8692                                     
REMARK   3      T33:   1.0051 T12:  -0.0339                                     
REMARK   3      T13:  -0.3204 T23:  -0.1591                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.1600 L22:  11.0135                                     
REMARK   3      L33:   7.9074 L12:   0.8590                                     
REMARK   3      L13:   3.8808 L23:  -1.0861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6505 S12:  -1.3229 S13:   1.7174                       
REMARK   3      S21:   1.3141 S22:  -0.3577 S23:  -2.7985                       
REMARK   3      S31:  -0.2945 S32:  -0.2064 S33:   1.0082                       
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 :   D    42        D   142                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3620  23.3060   8.1510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0185 T22:   0.6985                                     
REMARK   3      T33:   0.1685 T12:   0.0163                                     
REMARK   3      T13:  -0.1240 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.0425 L22:   8.3997                                     
REMARK   3      L33:   4.0383 L12:  -2.7963                                     
REMARK   3      L13:   1.2321 L23:  -1.6099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3390 S12:  -0.6686 S13:  -0.4856                       
REMARK   3      S21:   0.6390 S22:   0.6470 S23:  -0.4679                       
REMARK   3      S31:   0.1444 S32:  -0.5938 S33:  -0.3080                       
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 :   D   143        D   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7210  27.6040  21.8310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7324 T22:   2.1532                                     
REMARK   3      T33:   0.1882 T12:   0.6567                                     
REMARK   3      T13:   0.3783 T23:   0.3446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.4661 L22:   6.1698                                     
REMARK   3      L33:  13.1356 L12:  -2.1538                                     
REMARK   3      L13:   3.5139 L23:  -8.4987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6202 S12:  -3.3031 S13:   0.3035                       
REMARK   3      S21:   2.7791 S22:   1.5863 S23:   1.2105                       
REMARK   3      S31:  -0.8584 S32:  -1.6525 S33:  -0.9661                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050529.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-08; 15-OCT-07; 16-MAR-08    
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL; NULL                   
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y                            
REMARK 200  RADIATION SOURCE               : PAL/PLS; PAL/PLS; PAL/PLS          
REMARK 200  BEAMLINE                       : 4A; 6B; 6C1                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950, 0.97956, 0.97171;         
REMARK 200                                   0.97950, 0.97956, 0.97171;         
REMARK 200                                   0.97950, 0.97956, 0.97171          
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL                   
REMARK 200  OPTICS                         : NULL; NULL; NULL                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; CCD                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   210; ADSC QUANTUM 210              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; MAD; MAD                                  
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM/POTASSIUM TARTRATE, 15%      
REMARK 280  PEG 3350, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       32.03800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     SER A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     THR A    99                                                      
REMARK 465     SER A   100                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     VAL A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     THR A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     ASN A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     ALA A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     THR A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     GLN A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     GLN A   116                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     HIS B    20                                                      
REMARK 465     SER B    97                                                      
REMARK 465     LYS B    98                                                      
REMARK 465     THR B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     LYS B   101                                                      
REMARK 465     VAL B   102                                                      
REMARK 465     ARG B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     SER B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     ASN B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     THR B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     GLN B   114                                                      
REMARK 465     SER B   115                                                      
REMARK 465     GLN B   116                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     GLY C    13                                                      
REMARK 465     LEU C    14                                                      
REMARK 465     VAL C    15                                                      
REMARK 465     PRO C    16                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     HIS C    20                                                      
REMARK 465     MET C    21                                                      
REMARK 465     SER C    97                                                      
REMARK 465     LYS C    98                                                      
REMARK 465     THR C    99                                                      
REMARK 465     SER C   100                                                      
REMARK 465     LYS C   101                                                      
REMARK 465     VAL C   102                                                      
REMARK 465     ARG C   103                                                      
REMARK 465     PRO C   104                                                      
REMARK 465     SER C   105                                                      
REMARK 465     THR C   106                                                      
REMARK 465     GLY C   107                                                      
REMARK 465     ASN C   108                                                      
REMARK 465     SER C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     SER C   111                                                      
REMARK 465     THR C   112                                                      
REMARK 465     PRO C   113                                                      
REMARK 465     GLN C   114                                                      
REMARK 465     SER C   115                                                      
REMARK 465     GLN C   116                                                      
REMARK 465     LYS C   167                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     LEU D    14                                                      
REMARK 465     VAL D    15                                                      
REMARK 465     PRO D    16                                                      
REMARK 465     ARG D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     HIS D    20                                                      
REMARK 465     MET D    21                                                      
REMARK 465     SER D    97                                                      
REMARK 465     LYS D    98                                                      
REMARK 465     THR D    99                                                      
REMARK 465     SER D   100                                                      
REMARK 465     LYS D   101                                                      
REMARK 465     VAL D   102                                                      
REMARK 465     ARG D   103                                                      
REMARK 465     PRO D   104                                                      
REMARK 465     SER D   105                                                      
REMARK 465     THR D   106                                                      
REMARK 465     GLY D   107                                                      
REMARK 465     ASN D   108                                                      
REMARK 465     SER D   109                                                      
REMARK 465     ALA D   110                                                      
REMARK 465     SER D   111                                                      
REMARK 465     THR D   112                                                      
REMARK 465     PRO D   113                                                      
REMARK 465     GLN D   114                                                      
REMARK 465     SER D   115                                                      
REMARK 465     GLN D   116                                                      
REMARK 465     CYS D   117                                                      
REMARK 465     LYS D   166                                                      
REMARK 465     LYS D   167                                                      
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    PRO B  54        5.26    -69.47                                   
REMARK 500    LYS B  77       35.66     70.55                                   
REMARK 500    LYS C  93       -5.55    -57.17                                   
REMARK 500    ALA D  32      -71.80    -47.92                                   
REMARK 500    PRO D  54       -5.32    -58.94                                   
REMARK 500    LYS D  77       58.89    -68.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3FFL A   21   167  UNP    Q9UJX3   APC7_HUMAN       1    147             
DBREF  3FFL B   21   167  UNP    Q9UJX3   APC7_HUMAN       1    147             
DBREF  3FFL C   21   167  UNP    Q9UJX3   APC7_HUMAN       1    147             
DBREF  3FFL D   21   167  UNP    Q9UJX3   APC7_HUMAN       1    147             
SEQADV 3FFL MET A    1  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY A    2  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER A    3  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER A    4  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A    5  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A    6  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A    7  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A    8  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A    9  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A   10  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER A   11  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER A   12  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY A   13  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU A   14  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL VAL A   15  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL PRO A   16  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL ARG A   17  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY A   18  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER A   19  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS A   20  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU A   49  UNP  Q9UJX3    MET    29 ENGINEERED                     
SEQADV 3FFL LEU A  128  UNP  Q9UJX3    MET   108 ENGINEERED                     
SEQADV 3FFL VAL A  134  UNP  Q9UJX3    MET   114 ENGINEERED                     
SEQADV 3FFL LEU A  160  UNP  Q9UJX3    MET   140 ENGINEERED                     
SEQADV 3FFL MET B    1  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY B    2  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER B    3  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER B    4  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B    5  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B    6  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B    7  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B    8  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B    9  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B   10  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER B   11  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER B   12  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY B   13  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU B   14  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL VAL B   15  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL PRO B   16  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL ARG B   17  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY B   18  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER B   19  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS B   20  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU B   49  UNP  Q9UJX3    MET    29 ENGINEERED                     
SEQADV 3FFL LEU B  128  UNP  Q9UJX3    MET   108 ENGINEERED                     
SEQADV 3FFL VAL B  134  UNP  Q9UJX3    MET   114 ENGINEERED                     
SEQADV 3FFL LEU B  160  UNP  Q9UJX3    MET   140 ENGINEERED                     
SEQADV 3FFL MET C    1  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY C    2  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER C    3  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER C    4  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C    5  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C    6  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C    7  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C    8  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C    9  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C   10  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER C   11  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER C   12  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY C   13  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU C   14  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL VAL C   15  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL PRO C   16  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL ARG C   17  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY C   18  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER C   19  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS C   20  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU C   49  UNP  Q9UJX3    MET    29 ENGINEERED                     
SEQADV 3FFL LEU C  128  UNP  Q9UJX3    MET   108 ENGINEERED                     
SEQADV 3FFL VAL C  134  UNP  Q9UJX3    MET   114 ENGINEERED                     
SEQADV 3FFL LEU C  160  UNP  Q9UJX3    MET   140 ENGINEERED                     
SEQADV 3FFL MET D    1  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY D    2  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER D    3  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER D    4  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D    5  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D    6  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D    7  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D    8  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D    9  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D   10  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER D   11  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER D   12  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY D   13  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU D   14  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL VAL D   15  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL PRO D   16  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL ARG D   17  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL GLY D   18  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL SER D   19  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL HIS D   20  UNP  Q9UJX3              EXPRESSION TAG                 
SEQADV 3FFL LEU D   49  UNP  Q9UJX3    MET    29 ENGINEERED                     
SEQADV 3FFL LEU D  128  UNP  Q9UJX3    MET   108 ENGINEERED                     
SEQADV 3FFL VAL D  134  UNP  Q9UJX3    MET   114 ENGINEERED                     
SEQADV 3FFL LEU D  160  UNP  Q9UJX3    MET   140 ENGINEERED                     
SEQRES   1 A  167  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  167  LEU VAL PRO ARG GLY SER HIS MET ASN VAL ILE ASP HIS          
SEQRES   3 A  167  VAL ARG ASP MET ALA ALA ALA GLY LEU HIS SER ASN VAL          
SEQRES   4 A  167  ARG LEU LEU SER SER LEU LEU LEU THR LEU SER ASN ASN          
SEQRES   5 A  167  ASN PRO GLU LEU PHE SER PRO PRO GLN LYS TYR GLN LEU          
SEQRES   6 A  167  LEU VAL TYR HIS ALA ASP SER LEU PHE HIS ASP LYS GLU          
SEQRES   7 A  167  TYR ARG ASN ALA VAL SER LYS TYR THR MET ALA LEU GLN          
SEQRES   8 A  167  GLN LYS LYS ALA LEU SER LYS THR SER LYS VAL ARG PRO          
SEQRES   9 A  167  SER THR GLY ASN SER ALA SER THR PRO GLN SER GLN CYS          
SEQRES  10 A  167  LEU PRO SER GLU ILE GLU VAL LYS TYR LYS LEU ALA GLU          
SEQRES  11 A  167  CYS TYR THR VAL LEU LYS GLN ASP LYS ASP ALA ILE ALA          
SEQRES  12 A  167  ILE LEU ASP GLY ILE PRO SER ARG GLN ARG THR PRO LYS          
SEQRES  13 A  167  ILE ASN MET LEU LEU ALA ASN LEU TYR LYS LYS                  
SEQRES   1 B  167  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  167  LEU VAL PRO ARG GLY SER HIS MET ASN VAL ILE ASP HIS          
SEQRES   3 B  167  VAL ARG ASP MET ALA ALA ALA GLY LEU HIS SER ASN VAL          
SEQRES   4 B  167  ARG LEU LEU SER SER LEU LEU LEU THR LEU SER ASN ASN          
SEQRES   5 B  167  ASN PRO GLU LEU PHE SER PRO PRO GLN LYS TYR GLN LEU          
SEQRES   6 B  167  LEU VAL TYR HIS ALA ASP SER LEU PHE HIS ASP LYS GLU          
SEQRES   7 B  167  TYR ARG ASN ALA VAL SER LYS TYR THR MET ALA LEU GLN          
SEQRES   8 B  167  GLN LYS LYS ALA LEU SER LYS THR SER LYS VAL ARG PRO          
SEQRES   9 B  167  SER THR GLY ASN SER ALA SER THR PRO GLN SER GLN CYS          
SEQRES  10 B  167  LEU PRO SER GLU ILE GLU VAL LYS TYR LYS LEU ALA GLU          
SEQRES  11 B  167  CYS TYR THR VAL LEU LYS GLN ASP LYS ASP ALA ILE ALA          
SEQRES  12 B  167  ILE LEU ASP GLY ILE PRO SER ARG GLN ARG THR PRO LYS          
SEQRES  13 B  167  ILE ASN MET LEU LEU ALA ASN LEU TYR LYS LYS                  
SEQRES   1 C  167  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  167  LEU VAL PRO ARG GLY SER HIS MET ASN VAL ILE ASP HIS          
SEQRES   3 C  167  VAL ARG ASP MET ALA ALA ALA GLY LEU HIS SER ASN VAL          
SEQRES   4 C  167  ARG LEU LEU SER SER LEU LEU LEU THR LEU SER ASN ASN          
SEQRES   5 C  167  ASN PRO GLU LEU PHE SER PRO PRO GLN LYS TYR GLN LEU          
SEQRES   6 C  167  LEU VAL TYR HIS ALA ASP SER LEU PHE HIS ASP LYS GLU          
SEQRES   7 C  167  TYR ARG ASN ALA VAL SER LYS TYR THR MET ALA LEU GLN          
SEQRES   8 C  167  GLN LYS LYS ALA LEU SER LYS THR SER LYS VAL ARG PRO          
SEQRES   9 C  167  SER THR GLY ASN SER ALA SER THR PRO GLN SER GLN CYS          
SEQRES  10 C  167  LEU PRO SER GLU ILE GLU VAL LYS TYR LYS LEU ALA GLU          
SEQRES  11 C  167  CYS TYR THR VAL LEU LYS GLN ASP LYS ASP ALA ILE ALA          
SEQRES  12 C  167  ILE LEU ASP GLY ILE PRO SER ARG GLN ARG THR PRO LYS          
SEQRES  13 C  167  ILE ASN MET LEU LEU ALA ASN LEU TYR LYS LYS                  
SEQRES   1 D  167  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  167  LEU VAL PRO ARG GLY SER HIS MET ASN VAL ILE ASP HIS          
SEQRES   3 D  167  VAL ARG ASP MET ALA ALA ALA GLY LEU HIS SER ASN VAL          
SEQRES   4 D  167  ARG LEU LEU SER SER LEU LEU LEU THR LEU SER ASN ASN          
SEQRES   5 D  167  ASN PRO GLU LEU PHE SER PRO PRO GLN LYS TYR GLN LEU          
SEQRES   6 D  167  LEU VAL TYR HIS ALA ASP SER LEU PHE HIS ASP LYS GLU          
SEQRES   7 D  167  TYR ARG ASN ALA VAL SER LYS TYR THR MET ALA LEU GLN          
SEQRES   8 D  167  GLN LYS LYS ALA LEU SER LYS THR SER LYS VAL ARG PRO          
SEQRES   9 D  167  SER THR GLY ASN SER ALA SER THR PRO GLN SER GLN CYS          
SEQRES  10 D  167  LEU PRO SER GLU ILE GLU VAL LYS TYR LYS LEU ALA GLU          
SEQRES  11 D  167  CYS TYR THR VAL LEU LYS GLN ASP LYS ASP ALA ILE ALA          
SEQRES  12 D  167  ILE LEU ASP GLY ILE PRO SER ARG GLN ARG THR PRO LYS          
SEQRES  13 D  167  ILE ASN MET LEU LEU ALA ASN LEU TYR LYS LYS                  
FORMUL   5  HOH   *48(H2 O)                                                     
HELIX    1   1 ASN A   22  ALA A   33  1                                  12    
HELIX    2   2 LEU A   35  ASN A   53  1                                  19    
HELIX    3   3 SER A   58  ASP A   76  1                                  19    
HELIX    4   4 GLU A   78  ALA A   95  1                                  18    
HELIX    5   5 SER A  120  LEU A  135  1                                  16    
HELIX    6   6 GLN A  137  GLY A  147  1                                  11    
HELIX    7   7 PRO A  149  ARG A  153  5                                   5    
HELIX    8   8 THR A  154  TYR A  165  1                                  12    
HELIX    9   9 MET B   21  ALA B   33  1                                  13    
HELIX   10  10 LEU B   35  ASN B   53  1                                  19    
HELIX   11  11 SER B   58  ASP B   76  1                                  19    
HELIX   12  12 GLU B   78  LYS B   94  1                                  17    
HELIX   13  13 SER B  120  LEU B  135  1                                  16    
HELIX   14  14 GLN B  137  GLY B  147  1                                  11    
HELIX   15  15 PRO B  149  ARG B  153  5                                   5    
HELIX   16  16 THR B  154  TYR B  165  1                                  12    
HELIX   17  17 ASN C   22  GLY C   34  1                                  13    
HELIX   18  18 LEU C   35  ASN C   53  1                                  19    
HELIX   19  19 SER C   58  ASP C   76  1                                  19    
HELIX   20  20 GLU C   78  LYS C   94  1                                  17    
HELIX   21  21 SER C  120  LYS C  136  1                                  17    
HELIX   22  22 GLN C  137  GLY C  147  1                                  11    
HELIX   23  23 PRO C  149  ARG C  153  5                                   5    
HELIX   24  24 THR C  154  TYR C  165  1                                  12    
HELIX   25  25 ASN D   22  ALA D   33  1                                  12    
HELIX   26  26 LEU D   35  ASN D   51  1                                  17    
HELIX   27  27 SER D   58  ASP D   76  1                                  19    
HELIX   28  28 GLU D   78  ALA D   95  1                                  18    
HELIX   29  29 SER D  120  LEU D  135  1                                  16    
HELIX   30  30 GLN D  137  GLY D  147  1                                  11    
HELIX   31  31 THR D  154  LEU D  164  1                                  11    
CRYST1   80.493   64.076   81.597  90.00  95.23  90.00 P 1 21 1      8          
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      0.012423  0.000000  0.001137        0.00000                         
SCALE2      0.000000  0.015606  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012307        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system