GenomeNet

Database: PDB
Entry: 6FDK
LinkDB: 6FDK
Original site: 6FDK 
HEADER    HYDROLASE                               25-DEC-17   6FDK              
TITLE     STRUCTURE OF CHLAMYDIA TRACHOMATIS EFFECTOR PROTEIN CDU1 BOUND TO     
TITLE    2 UBIQUITIN                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEUBIQUITINASE AND DENEDDYLASE DUB1;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CHLADUB1;                                                   
COMPND   5 EC: 3.4.22.-;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: POLYUBIQUITIN-B;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDIA TRACHOMATIS 434/BU;                   
SOURCE   3 ORGANISM_TAXID: 471472;                                              
SOURCE   4 GENE: CDU1, CTL0247;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: UBB;                                                           
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    CHLADUB1, CE PROTEASE, DUB, UBIQUITIN., HYDROLASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.RAMIREZ,C.KISKER                                                    
REVDAT   4   07-FEB-24 6FDK    1       REMARK                                   
REVDAT   3   15-MAR-23 6FDK    1       COMPND SOURCE REMARK DBREF               
REVDAT   3 2                   1       SEQRES LINK   ATOM                       
REVDAT   2   17-OCT-18 6FDK    1       JRNL                                     
REVDAT   1   15-AUG-18 6FDK    0                                                
JRNL        AUTH   Y.A.RAMIREZ,T.B.ADLER,E.ALTMANN,T.KLEMM,C.TIESMEYER,F.SAUER, 
JRNL        AUTH 2 S.G.KATHMAN,A.V.STATSYUK,C.SOTRIFFER,C.KISKER                
JRNL        TITL   STRUCTURAL BASIS OF SUBSTRATE RECOGNITION AND COVALENT       
JRNL        TITL 2 INHIBITION OF CDU1 FROM CHLAMYDIA TRACHOMATIS.               
JRNL        REF    CHEMMEDCHEM                   V.  13  2014 2018              
JRNL        REFN                   ESSN 1860-7187                               
JRNL        PMID   30028574                                                     
JRNL        DOI    10.1002/CMDC.201800364                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39198                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2021                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2895                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.6290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.6760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2543                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 423                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : -0.19000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.35000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.352         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2642 ; 0.030 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2501 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3594 ; 2.530 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5833 ; 1.287 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   324 ; 6.224 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;35.692 ;24.569       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   473 ;14.169 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.026 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   403 ; 0.190 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2881 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   517 ; 0.002 ; 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):  1276 ; 1.640 ; 1.778       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1275 ; 1.638 ; 1.778       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1594 ; 2.301 ; 2.665       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1595 ; 2.300 ; 2.665       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1366 ; 3.047 ; 2.091       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1367 ; 3.046 ; 2.091       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1996 ; 4.544 ; 2.998       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2953 ; 6.377 ;22.952       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2954 ; 6.376 ;22.948       
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   162        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1819 -61.2663  73.2128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0503 T22:   0.0396                                     
REMARK   3      T33:   0.0132 T12:   0.0034                                     
REMARK   3      T13:  -0.0034 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9189 L22:   0.3147                                     
REMARK   3      L33:   0.0099 L12:   0.2247                                     
REMARK   3      L13:  -0.0019 L23:  -0.0209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0054 S12:   0.0772 S13:   0.0951                       
REMARK   3      S21:  -0.0119 S22:   0.0028 S23:   0.0218                       
REMARK   3      S31:  -0.0013 S32:   0.0170 S33:  -0.0082                       
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   199        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8426 -71.6318  71.0511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0494 T22:   0.0266                                     
REMARK   3      T33:   0.0018 T12:   0.0089                                     
REMARK   3      T13:  -0.0026 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5858 L22:   0.1195                                     
REMARK   3      L33:   0.1634 L12:  -0.0586                                     
REMARK   3      L13:   0.2468 L23:  -0.1068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:   0.0267 S13:  -0.0284                       
REMARK   3      S21:  -0.0079 S22:  -0.0033 S23:  -0.0030                       
REMARK   3      S31:   0.0097 S32:   0.0144 S33:  -0.0062                       
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   283        A   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2645 -77.3230  79.6119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0358 T22:   0.0303                                     
REMARK   3      T33:   0.0217 T12:  -0.0004                                     
REMARK   3      T13:  -0.0083 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7425 L22:   0.4890                                     
REMARK   3      L33:   0.9708 L12:  -0.5264                                     
REMARK   3      L13:   0.7170 L23:  -0.3827                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0216 S12:  -0.0272 S13:  -0.0983                       
REMARK   3      S21:   0.0130 S22:   0.0520 S23:   0.0786                       
REMARK   3      S31:   0.0123 S32:  -0.0266 S33:  -0.0736                       
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 :   A   332        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2576 -56.8461  77.3477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0510 T22:   0.0076                                     
REMARK   3      T33:   0.0512 T12:   0.0121                                     
REMARK   3      T13:   0.0176 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7947 L22:   0.2925                                     
REMARK   3      L33:   0.1185 L12:   0.0694                                     
REMARK   3      L13:   0.0390 L23:  -0.1418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0630 S12:  -0.0168 S13:   0.1355                       
REMARK   3      S21:   0.0396 S22:  -0.0113 S23:   0.0625                       
REMARK   3      S31:  -0.0119 S32:  -0.0070 S33:  -0.0516                       
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   155        B   198                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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   199        B   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   216        B   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   239        B   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   255        B   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   283        B   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   332        B   371                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
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 :   B   372        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0269                                     
REMARK   3      T33:   0.0269 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6FDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200008135.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41326                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.320                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5B5Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: BLADE LIKE                                                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 12% PEG 20000, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293.15K                        
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       28.46850            
REMARK 290   SMTRY3   2  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   136                                                      
REMARK 465     LYS A   137                                                      
REMARK 465     HIS A   138                                                      
REMARK 465     HIS A   139                                                      
REMARK 465     HIS A   140                                                      
REMARK 465     HIS A   141                                                      
REMARK 465     HIS A   142                                                      
REMARK 465     HIS A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     ALA A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     VAL A   149                                                      
REMARK 465     LEU A   150                                                      
REMARK 465     PHE A   151                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     PRO A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     ILE A   159                                                      
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   NE2  GLN A   237     O    HOH A   601              2.07            
REMARK 500   O    HOH A   649     O    HOH A   834              2.10            
REMARK 500   O    HOH A   609     O    HOH A   750              2.11            
REMARK 500   O    HOH A   614     O    HOH A   754              2.13            
REMARK 500   O    HOH A   697     O    HOH A   834              2.17            
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    GLU A 189   CD    GLU A 189   OE1     0.102                       
REMARK 500    GLU A 217   CD    GLU A 217   OE1     0.075                       
REMARK 500    TYR A 232   CZ    TYR A 232   CE2     0.078                       
REMARK 500    SER A 256   CA    SER A 256   CB      0.103                       
REMARK 500    LEU A 288   C     LEU A 288   O       0.117                       
REMARK 500    SER A 324   N     SER A 324   CA      0.450                       
REMARK 500    SER A 324   CA    SER A 324   CB      0.141                       
REMARK 500    SER A 324   CB    SER A 324   OG      0.091                       
REMARK 500    ASP A 367   CB    ASP A 367   CG      0.133                       
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    ASP A 169   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    PHE A 191   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    LEU A 277   CB  -  CG  -  CD1 ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ARG A 286   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 286   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 287   CD  -  NE  -  CZ  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH1 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASP A 323   O   -  C   -  N   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    SER A 324   C   -  N   -  CA  ANGL. DEV. = -29.2 DEGREES          
REMARK 500    SER A 324   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    SER A 324   N   -  CA  -  CB  ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ASP A 359   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 367   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 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    TYR A 295      -50.66     72.68                                   
REMARK 500    ASN A 296       34.38   -142.71                                   
REMARK 500    SER A 324      -23.98     99.14                                   
REMARK 500    ASP A 359      108.87   -162.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 287         0.09    SIDE CHAIN                              
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 CL A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYE A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5B5Q   RELATED DB: PDB                                   
REMARK 900 LIGAND-FREE PROTEIN                                                  
REMARK 900 RELATED ID: 5HAG   RELATED DB: PDB                                   
REMARK 900 LIGAND-FREE PROTEIN                                                  
DBREF  6FDK A  155   401  UNP    B0B9A0   CDUB1_CHLT2    155    401             
DBREF  6FDK B    1    75  UNP    P0CG47   UBB_HUMAN        1     75             
SEQADV 6FDK MET A  136  UNP  B0B9A0              INITIATING METHIONINE          
SEQADV 6FDK LYS A  137  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  138  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  139  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  140  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  141  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  142  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK HIS A  143  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK SER A  144  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK ALA A  145  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK GLY A  146  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK LEU A  147  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK GLU A  148  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK VAL A  149  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK LEU A  150  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK PHE A  151  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK GLN A  152  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK GLY A  153  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK PRO A  154  UNP  B0B9A0              EXPRESSION TAG                 
SEQADV 6FDK ALA A  174  UNP  B0B9A0    CYS   174 ENGINEERED MUTATION            
SEQADV 6FDK SER A  226  UNP  B0B9A0    CYS   226 ENGINEERED MUTATION            
SEQADV 6FDK ALA A  386  UNP  B0B9A0    CYS   386 ENGINEERED MUTATION            
SEQRES   1 A  266  MET LYS HIS HIS HIS HIS HIS HIS SER ALA GLY LEU GLU          
SEQRES   2 A  266  VAL LEU PHE GLN GLY PRO ARG ARG GLN THR ILE GLU ALA          
SEQRES   3 A  266  LEU VAL PRO ALA TRP ASP SER ASP ILE ILE PHE LYS ALA          
SEQRES   4 A  266  LEU CYS TYR PHE HIS THR LEU TYR PRO GLY LEU ILE PRO          
SEQRES   5 A  266  LEU GLU THR PHE PRO PRO ALA THR ILE PHE ASN PHE LYS          
SEQRES   6 A  266  GLN LYS ILE ILE SER ILE LEU GLU ASP LYS LYS ALA VAL          
SEQRES   7 A  266  LEU ARG GLY GLU PRO ILE LYS GLY PRO LEU PRO ILE SER          
SEQRES   8 A  266  CYS SER LYS GLU ASN TYR ARG ARG HIS LEU GLN ARG THR          
SEQRES   9 A  266  THR LEU LEU PRO VAL PHE MET TRP TYR HIS PRO THR PRO          
SEQRES  10 A  266  LYS THR LEU SER ASP THR MET GLN THR MET LYS GLN LEU          
SEQRES  11 A  266  ALA ILE LYS GLY SER VAL GLY ALA SER HIS TRP LEU LEU          
SEQRES  12 A  266  VAL ILE VAL ASP ILE GLN ALA ARG ARG LEU VAL TYR PHE          
SEQRES  13 A  266  ASP SER LEU TYR ASN TYR VAL MET PRO PRO GLU ASN MET          
SEQRES  14 A  266  LYS LYS GLU LEU GLN SER PHE ALA GLN GLN LEU ASP GLN          
SEQRES  15 A  266  VAL TYR PRO ALA TYR ASP SER LYS LYS PHE SER VAL LYS          
SEQRES  16 A  266  ILE ALA ALA LYS GLU VAL ILE GLN ARG GLY SER GLY SER          
SEQRES  17 A  266  SER CYS GLY ALA TRP CYS CYS GLN PHE LEU HIS TRP TYR          
SEQRES  18 A  266  LEU LYS ASP PRO LEU THR ASP ALA LEU ASN ASP LEU PRO          
SEQRES  19 A  266  VAL ASP SER VAL GLU ARG HIS GLU ASN LEU ALA SER PHE          
SEQRES  20 A  266  VAL GLN ALA ALA GLU ALA ALA VAL GLN ASP LEU PRO GLU          
SEQRES  21 A  266  LEU SER TRP PRO GLU ALA                                      
SEQRES   1 B   75  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   75  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 B   75  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   75  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   75  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   75  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY                      
HET     CL  A 501       1                                                       
HET    AYE  A 502       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     AYE PROP-2-EN-1-AMINE                                                
HETSYN     AYE ALLYLAMINE                                                       
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  AYE    C3 H7 N                                                      
FORMUL   5  HOH   *423(H2 O)                                                    
HELIX    1 AA1 ASP A  167  TYR A  182  1                                  16    
HELIX    2 AA2 ASN A  198  ARG A  215  1                                  18    
HELIX    3 AA3 SER A  228  THR A  239  1                                  12    
HELIX    4 AA4 THR A  254  GLY A  269  1                                  16    
HELIX    5 AA5 PRO A  300  TYR A  319  1                                  20    
HELIX    6 AA6 SER A  344  ASP A  359  1                                  16    
HELIX    7 AA7 ASP A  363  ASP A  367  5                                   5    
HELIX    8 AA8 ASP A  371  GLN A  391  1                                  21    
HELIX    9 AA9 THR B   22  GLY B   35  1                                  14    
HELIX   10 AB1 PRO B   37  GLN B   41  5                                   5    
HELIX   11 AB2 THR B   55  ASN B   60  5                                   6    
SHEET    1 AA1 4 LEU A 241  TYR A 248  0                                        
SHEET    2 AA1 4 HIS A 275  ASP A 282 -1  O  LEU A 277   N  MET A 246           
SHEET    3 AA1 4 ARG A 287  PHE A 291 -1  O  ARG A 287   N  ASP A 282           
SHEET    4 AA1 4 SER A 328  ILE A 331  1  O  LYS A 330   N  LEU A 288           
SHEET    1 AA2 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA2 5 GLN B   2  LYS B   6 -1  N  VAL B   5   O  ILE B  13           
SHEET    3 AA2 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4 AA2 5 ARG B  42  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5 AA2 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
LINK         SG  CYS A 345                 C2  AYE A 502     1555   1555  1.76  
LINK         N1  AYE A 502                 C   GLY B  75     1555   1555  1.36  
CISPEP   1 PHE A  191    PRO A  192          0         5.97                     
CISPEP   2 GLY A  221    PRO A  222          0         3.37                     
SITE     1 AC1  5 PRO A 183  LEU A 185  ILE A 186  HIS A 235                    
SITE     2 AC1  5 THR A 239                                                     
SITE     1 AC2  6 VAL A 271  SER A 274  HIS A 275  GLY A 342                    
SITE     2 AC2  6 CYS A 345  GLY B  75                                          
CRYST1   47.815   56.937   60.695  90.00 104.86  90.00 P 1 21 1      2          
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      0.020914  0.000000  0.005550        0.00000                         
SCALE2      0.000000  0.017563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017046        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system