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Database: PDB
Entry: 3BXE
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HEADER    GENE REGULATION                         13-JAN-08   3BXE              
TITLE     CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC    
TITLE    2 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN COMPLEX WITH         
TITLE    3 DIHYDROXYACETONE PHOSPHATE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CENTRAL GLYCOLYTIC GENE REGULATOR;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EFFECTOR BINDING DOMAIN: RESIDUES 89-340;                  
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: CGGR, YVBQ, BSU33950;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    EFFECTOR BINDING DOMAIN, CATABOLIC REPRESSOR, TRANSCRIPTIONAL         
KEYWDS   2 REGULATOR, DEOR FAMILY, DNA-BINDING, TRANSCRIPTION REGULATION, GENE  
KEYWDS   3 REGULATION                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.REZACOVA,Z.OTWINOWSKI                                               
REVDAT   6   13-JUL-11 3BXE    1       VERSN                                    
REVDAT   5   09-JUN-09 3BXE    1       REVDAT                                   
REVDAT   4   24-FEB-09 3BXE    1       VERSN                                    
REVDAT   3   06-JAN-09 3BXE    1       JRNL                                     
REVDAT   2   19-AUG-08 3BXE    1       JRNL                                     
REVDAT   1   01-JUL-08 3BXE    0                                                
JRNL        AUTH   P.REZACOVA,M.KOZISEK,S.F.MOY,I.SIEGLOVA,A.JOACHIMIAK,        
JRNL        AUTH 2 M.MACHIUS,Z.OTWINOWSKI                                       
JRNL        TITL   CRYSTAL STRUCTURES OF THE EFFECTOR-BINDING DOMAIN OF         
JRNL        TITL 2 REPRESSOR CENTRAL GLYCOLYTIC GENE REGULATOR FROM BACILLUS    
JRNL        TITL 3 SUBTILIS REVEAL LIGAND-INDUCED STRUCTURAL CHANGES UPON       
JRNL        TITL 4 BINDING OF SEVERAL GLYCOLYTIC INTERMEDIATES.                 
JRNL        REF    MOL.MICROBIOL.                V.  69   895 2008              
JRNL        REFN                   ISSN 0950-382X                               
JRNL        PMID   18554327                                                     
JRNL        DOI    10.1111/J.1365-2958.2008.06318.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 47018                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2517                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3185                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 169                          
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3786                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 603                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 33.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.34000                                              
REMARK   3    B22 (A**2) : -0.81000                                             
REMARK   3    B33 (A**2) : 0.47000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.971         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3954 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5354 ; 1.234 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   533 ; 5.028 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   164 ;38.744 ;25.427       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   744 ;12.699 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;13.041 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   618 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2919 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1946 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2747 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   506 ; 0.149 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    65 ; 0.167 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.136 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2615 ; 0.644 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4076 ; 1.028 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1484 ; 1.922 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1261 ; 3.139 ; 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  : 15                                         
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    93        A   103                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.3040   8.8340  27.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0953 T22:   0.0194                                     
REMARK   3      T33:  -0.1529 T12:   0.0286                                     
REMARK   3      T13:   0.0212 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2286 L22:  12.0257                                     
REMARK   3      L33:   7.3393 L12:   2.3713                                     
REMARK   3      L13:   0.3483 L23:  -0.5676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1005 S12:  -0.4463 S13:   0.5621                       
REMARK   3      S21:   0.4303 S22:   0.1350 S23:   0.0021                       
REMARK   3      S31:  -0.5448 S32:  -0.2161 S33:  -0.0345                       
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   104        A   126                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.8770  10.5270  15.9230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1548 T22:  -0.0941                                     
REMARK   3      T33:  -0.1467 T12:   0.0083                                     
REMARK   3      T13:   0.0028 T23:  -0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1457 L22:   3.8351                                     
REMARK   3      L33:   3.8461 L12:   0.1678                                     
REMARK   3      L13:   0.1510 L23:  -1.8684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0014 S12:  -0.0112 S13:   0.1773                       
REMARK   3      S21:  -0.0713 S22:  -0.0186 S23:   0.1609                       
REMARK   3      S31:  -0.1156 S32:  -0.0041 S33:   0.0172                       
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   127        A   176                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5900   4.3630  11.0130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1238 T22:  -0.0774                                     
REMARK   3      T33:  -0.1756 T12:  -0.0163                                     
REMARK   3      T13:   0.0137 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6670 L22:   1.8026                                     
REMARK   3      L33:   2.0706 L12:  -0.1629                                     
REMARK   3      L13:  -0.0536 L23:   0.4289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0578 S12:  -0.0149 S13:   0.0734                       
REMARK   3      S21:   0.0011 S22:   0.0970 S23:  -0.1701                       
REMARK   3      S31:  -0.0385 S32:   0.1426 S33:  -0.0392                       
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   177        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2440   1.6210   0.0150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0712 T22:  -0.0272                                     
REMARK   3      T33:  -0.1915 T12:  -0.0043                                     
REMARK   3      T13:   0.0287 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8304 L22:   2.9925                                     
REMARK   3      L33:   2.6246 L12:   2.8036                                     
REMARK   3      L13:   1.5969 L23:   1.0564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1325 S12:   0.4581 S13:   0.0708                       
REMARK   3      S21:  -0.2028 S22:   0.1231 S23:  -0.0841                       
REMARK   3      S31:  -0.0837 S32:   0.1046 S33:   0.0094                       
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 :   A   203        A   224                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8190 -15.4160  -6.6160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0443 T22:   0.0651                                     
REMARK   3      T33:  -0.0231 T12:  -0.0374                                     
REMARK   3      T13:   0.0722 T23:  -0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5674 L22:   9.4393                                     
REMARK   3      L33:   7.7612 L12:   3.1802                                     
REMARK   3      L13:   2.6200 L23:   4.8469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0211 S12:  -0.0743 S13:   0.0584                       
REMARK   3      S21:   0.0496 S22:  -0.1116 S23:   0.6244                       
REMARK   3      S31:   0.4756 S32:  -0.4719 S33:   0.1327                       
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 :   A   225        A   251                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6770  -5.5630   5.9900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0784 T22:  -0.1151                                     
REMARK   3      T33:  -0.1922 T12:  -0.0430                                     
REMARK   3      T13:   0.0155 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3387 L22:   1.5765                                     
REMARK   3      L33:   2.0992 L12:   0.0401                                     
REMARK   3      L13:   0.3096 L23:   0.1997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1198 S12:   0.0368 S13:  -0.1098                       
REMARK   3      S21:  -0.1552 S22:   0.0934 S23:   0.0292                       
REMARK   3      S31:   0.2191 S32:  -0.0737 S33:   0.0264                       
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 :   A   252        A   284                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.7690  -9.6210   5.5980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0732 T22:  -0.0425                                     
REMARK   3      T33:  -0.1509 T12:  -0.0612                                     
REMARK   3      T13:  -0.0055 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9589 L22:   3.1014                                     
REMARK   3      L33:   3.2557 L12:   0.5621                                     
REMARK   3      L13:   2.4422 L23:   1.3860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0085 S12:   0.0893 S13:  -0.0358                       
REMARK   3      S21:  -0.1423 S22:   0.0059 S23:   0.1485                       
REMARK   3      S31:   0.2898 S32:  -0.0746 S33:  -0.0145                       
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 :   A   285        A   309                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.6970  -6.9140  11.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0909 T22:  -0.0616                                     
REMARK   3      T33:  -0.1655 T12:  -0.0235                                     
REMARK   3      T13:   0.0172 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3404 L22:   1.5395                                     
REMARK   3      L33:   0.9127 L12:   0.0016                                     
REMARK   3      L13:  -0.2532 L23:   0.0404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1398 S12:   0.0895 S13:  -0.2453                       
REMARK   3      S21:  -0.0197 S22:   0.0717 S23:  -0.0672                       
REMARK   3      S31:   0.1801 S32:  -0.0934 S33:   0.0681                       
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 :   A   310        A   335                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.2270   2.0220  17.7980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1590 T22:  -0.0670                                     
REMARK   3      T33:  -0.2048 T12:  -0.0227                                     
REMARK   3      T13:   0.0078 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1423 L22:   2.4667                                     
REMARK   3      L33:   2.4275 L12:  -0.0639                                     
REMARK   3      L13:   0.1306 L23:  -0.5440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0298 S12:  -0.1090 S13:   0.0056                       
REMARK   3      S21:   0.0942 S22:  -0.0278 S23:   0.1330                       
REMARK   3      S31:   0.0098 S32:  -0.2250 S33:  -0.0020                       
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 :   A   336        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A): -54.3330   9.3760  22.4930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1118 T22:  -0.0393                                     
REMARK   3      T33:  -0.1133 T12:   0.0167                                     
REMARK   3      T13:   0.0013 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.2691 L22:  19.2484                                     
REMARK   3      L33:  36.8360 L12:  -3.7512                                     
REMARK   3      L13:  -7.2425 L23:  10.7278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0085 S12:  -0.2020 S13:   0.6532                       
REMARK   3      S21:  -0.2270 S22:   0.0109 S23:   0.5317                       
REMARK   3      S31:  -0.9960 S32:  -0.2698 S33:  -0.0193                       
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    86        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8540  14.7890 -21.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1201 T22:  -0.0387                                     
REMARK   3      T33:  -0.1089 T12:  -0.0078                                     
REMARK   3      T13:   0.0076 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2487 L22:   2.9831                                     
REMARK   3      L33:   2.8955 L12:  -0.1983                                     
REMARK   3      L13:  -0.4168 L23:   0.7597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0209 S12:   0.0536 S13:   0.0904                       
REMARK   3      S21:  -0.0295 S22:   0.0001 S23:  -0.2000                       
REMARK   3      S31:  -0.0060 S32:   0.0448 S33:  -0.0210                       
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   123        B   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8900  10.2690 -19.7620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1504 T22:  -0.1045                                     
REMARK   3      T33:  -0.1595 T12:  -0.0015                                     
REMARK   3      T13:   0.0086 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8653 L22:   1.7402                                     
REMARK   3      L33:   0.9898 L12:   0.6687                                     
REMARK   3      L13:   0.5032 L23:  -0.0507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0221 S12:   0.0279 S13:   0.1489                       
REMARK   3      S21:   0.0064 S22:   0.0115 S23:   0.1454                       
REMARK   3      S31:  -0.0241 S32:   0.0021 S33:   0.0106                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   157        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2540   7.8640 -20.2600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0982 T22:  -0.0807                                     
REMARK   3      T33:  -0.1190 T12:   0.0027                                     
REMARK   3      T13:   0.0245 T23:   0.0177                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9588 L22:   2.9772                                     
REMARK   3      L33:   2.0480 L12:  -0.0849                                     
REMARK   3      L13:   0.2893 L23:   0.4836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:  -0.0336 S13:   0.1820                       
REMARK   3      S21:  -0.2166 S22:  -0.0464 S23:   0.1884                       
REMARK   3      S31:  -0.1329 S32:  -0.0992 S33:   0.0487                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   178        B   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1010   1.6810 -11.9770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0860 T22:  -0.0511                                     
REMARK   3      T33:  -0.1720 T12:  -0.0261                                     
REMARK   3      T13:   0.0330 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9148 L22:   5.0007                                     
REMARK   3      L33:   2.4337 L12:  -2.7220                                     
REMARK   3      L13:   1.1704 L23:  -1.8025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:  -0.1729 S13:  -0.0002                       
REMARK   3      S21:   0.2372 S22:  -0.0458 S23:   0.2249                       
REMARK   3      S31:  -0.0063 S32:  -0.1201 S33:   0.0437                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   203        B   219                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5370 -16.9740 -13.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1305 T22:   0.0777                                     
REMARK   3      T33:  -0.0488 T12:   0.0489                                     
REMARK   3      T13:   0.0270 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3219 L22:  17.5743                                     
REMARK   3      L33:   1.1860 L12:  -4.3450                                     
REMARK   3      L13:   0.9011 L23:  -4.4965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0706 S12:   0.1350 S13:  -0.0205                       
REMARK   3      S21:   0.0129 S22:  -0.0528 S23:  -0.1162                       
REMARK   3      S31:   0.0541 S32:   0.1880 S33:  -0.0178                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ DW                    
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OKG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 0.2M AMMONIUM FORMATE PH      
REMARK 280  6.6, 20% (W/V) PEG 3350. 25MG/ML PROTEIN WITH 10MM GLYCERALDEHYDE   
REMARK 280  -3-PHOSPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.76850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.85600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.91100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.85600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.76850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.91100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AUTHORS STATE THAT THE DIMERIC ASSEMBLY OF THE BIOLOGICAL    
REMARK 300 UNIT THAT IS SHOWN IN REMARK 350 IS PUTATIVE AT THE TIME OF          
REMARK 300 DEPOSITION.                                                          
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: 1210 ANGSTROM**2                          
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     SER A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     LYS A    89                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     VAL A    91                                                      
REMARK 465     LEU A    92                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     GLU B   340                                                      
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    GLN A 209       73.04   -103.28                                   
REMARK 500    ASN A 252       48.41    -99.13                                   
REMARK 500    PHE A 271       43.38     39.44                                   
REMARK 500    SER A 287      142.53   -171.36                                   
REMARK 500    SER B 140     -162.56   -110.25                                   
REMARK 500    PHE B 205       78.49   -118.79                                   
REMARK 500    ASN B 252       45.16    -91.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 649        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 639        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH B 703        DISTANCE =  5.88 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OKG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL              
REMARK 900 GLYCOLYTIC GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS              
REMARK 900 RELATED ID: 3BXF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL              
REMARK 900 GLYCOLYTIC GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN           
REMARK 900 COMPLEX WITH EFFECTOR FRUCTOSE-1,6-BISPHOSPHATE                      
REMARK 900 RELATED ID: 3BXG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL              
REMARK 900 GLYCOLYTIC GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN           
REMARK 900 COMPLEX WITH GLUCOSE-6-PHOSPHATE                                     
REMARK 900 RELATED ID: 3BXH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL              
REMARK 900 GLYCOLYTIC GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN           
REMARK 900 COMPLEX WITH FRUCTOSE-6-PHOSPHATE                                    
DBREF  3BXE A   89   340  UNP    O32253   CGGR_BACSU      89    340             
DBREF  3BXE B   89   340  UNP    O32253   CGGR_BACSU      89    340             
SEQADV 3BXE SER A   86  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXE ASN A   87  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXE ALA A   88  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXE SER B   86  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXE ASN B   87  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXE ALA B   88  UNP  O32253              EXPRESSION TAG                 
SEQRES   1 A  255  SER ASN ALA LYS ASP VAL LEU GLY LEU THR LEU LEU GLU          
SEQRES   2 A  255  LYS THR LEU LYS GLU ARG LEU ASN LEU LYS ASP ALA ILE          
SEQRES   3 A  255  ILE VAL SER GLY ASP SER ASP GLN SER PRO TRP VAL LYS          
SEQRES   4 A  255  LYS GLU MET GLY ARG ALA ALA VAL ALA CYS MET LYS LYS          
SEQRES   5 A  255  ARG PHE SER GLY LYS ASN ILE VAL ALA VAL THR GLY GLY          
SEQRES   6 A  255  THR THR ILE GLU ALA VAL ALA GLU MET MET THR PRO ASP          
SEQRES   7 A  255  SER LYS ASN ARG GLU LEU LEU PHE VAL PRO ALA ARG GLY          
SEQRES   8 A  255  GLY LEU GLY GLU ASP VAL LYS ASN GLN ALA ASN THR ILE          
SEQRES   9 A  255  CYS ALA HIS MET ALA GLU LYS ALA SER GLY THR TYR ARG          
SEQRES  10 A  255  LEU LEU PHE VAL PRO GLY GLN LEU SER GLN GLY ALA TYR          
SEQRES  11 A  255  SER SER ILE ILE GLU GLU PRO SER VAL LYS GLU VAL LEU          
SEQRES  12 A  255  ASN THR ILE LYS SER ALA SER MET LEU VAL HIS GLY ILE          
SEQRES  13 A  255  GLY GLU ALA LYS THR MET ALA GLN ARG ARG ASN THR PRO          
SEQRES  14 A  255  LEU GLU ASP LEU LYS LYS ILE ASP ASP ASN ASP ALA VAL          
SEQRES  15 A  255  THR GLU ALA PHE GLY TYR TYR PHE ASN ALA ASP GLY GLU          
SEQRES  16 A  255  VAL VAL HIS LYS VAL HIS SER VAL GLY MET GLN LEU ASP          
SEQRES  17 A  255  ASP ILE ASP ALA ILE PRO ASP ILE ILE ALA VAL ALA GLY          
SEQRES  18 A  255  GLY SER SER LYS ALA GLU ALA ILE GLU ALA TYR PHE LYS          
SEQRES  19 A  255  LYS PRO ARG ASN THR VAL LEU VAL THR ASP GLU GLY ALA          
SEQRES  20 A  255  ALA LYS LYS LEU LEU ARG ASP GLU                              
SEQRES   1 B  255  SER ASN ALA LYS ASP VAL LEU GLY LEU THR LEU LEU GLU          
SEQRES   2 B  255  LYS THR LEU LYS GLU ARG LEU ASN LEU LYS ASP ALA ILE          
SEQRES   3 B  255  ILE VAL SER GLY ASP SER ASP GLN SER PRO TRP VAL LYS          
SEQRES   4 B  255  LYS GLU MET GLY ARG ALA ALA VAL ALA CYS MET LYS LYS          
SEQRES   5 B  255  ARG PHE SER GLY LYS ASN ILE VAL ALA VAL THR GLY GLY          
SEQRES   6 B  255  THR THR ILE GLU ALA VAL ALA GLU MET MET THR PRO ASP          
SEQRES   7 B  255  SER LYS ASN ARG GLU LEU LEU PHE VAL PRO ALA ARG GLY          
SEQRES   8 B  255  GLY LEU GLY GLU ASP VAL LYS ASN GLN ALA ASN THR ILE          
SEQRES   9 B  255  CYS ALA HIS MET ALA GLU LYS ALA SER GLY THR TYR ARG          
SEQRES  10 B  255  LEU LEU PHE VAL PRO GLY GLN LEU SER GLN GLY ALA TYR          
SEQRES  11 B  255  SER SER ILE ILE GLU GLU PRO SER VAL LYS GLU VAL LEU          
SEQRES  12 B  255  ASN THR ILE LYS SER ALA SER MET LEU VAL HIS GLY ILE          
SEQRES  13 B  255  GLY GLU ALA LYS THR MET ALA GLN ARG ARG ASN THR PRO          
SEQRES  14 B  255  LEU GLU ASP LEU LYS LYS ILE ASP ASP ASN ASP ALA VAL          
SEQRES  15 B  255  THR GLU ALA PHE GLY TYR TYR PHE ASN ALA ASP GLY GLU          
SEQRES  16 B  255  VAL VAL HIS LYS VAL HIS SER VAL GLY MET GLN LEU ASP          
SEQRES  17 B  255  ASP ILE ASP ALA ILE PRO ASP ILE ILE ALA VAL ALA GLY          
SEQRES  18 B  255  GLY SER SER LYS ALA GLU ALA ILE GLU ALA TYR PHE LYS          
SEQRES  19 B  255  LYS PRO ARG ASN THR VAL LEU VAL THR ASP GLU GLY ALA          
SEQRES  20 B  255  ALA LYS LYS LEU LEU ARG ASP GLU                              
HET    13P  A 401      10                                                       
HET    13P  B 401      10                                                       
HETNAM     13P 1,3-DIHYDROXYACETONEPHOSPHATE                                    
FORMUL   3  13P    2(C3 H7 O6 P)                                                
FORMUL   5  HOH   *603(H2 O)                                                    
HELIX    1   1 GLY A   93  ASN A  106  1                                  14    
HELIX    2   2 TRP A  122  PHE A  139  1                                  18    
HELIX    3   3 GLY A  150  MET A  160  1                                  11    
HELIX    4   4 ASP A  181  ASN A  184  5                                   4    
HELIX    5   5 GLN A  185  ALA A  197  1                                  13    
HELIX    6   6 SER A  211  GLU A  221  1                                  11    
HELIX    7   7 GLU A  221  SER A  233  1                                  13    
HELIX    8   8 ALA A  244  ARG A  251  1                                   8    
HELIX    9   9 PRO A  254  ASN A  264  1                                  11    
HELIX   10  10 GLN A  291  ILE A  298  5                                   8    
HELIX   11  11 GLY A  307  SER A  309  5                                   3    
HELIX   12  12 LYS A  310  PHE A  318  1                                   9    
HELIX   13  13 GLU A  330  ARG A  338  1                                   9    
HELIX   14  14 SER B   86  LEU B   92  1                                   7    
HELIX   15  15 GLY B   93  ASN B  106  1                                  14    
HELIX   16  16 PRO B  121  PHE B  139  1                                  19    
HELIX   17  17 GLY B  150  MET B  160  1                                  11    
HELIX   18  18 ASP B  181  ASN B  184  5                                   4    
HELIX   19  19 GLN B  185  SER B  198  1                                  14    
HELIX   20  20 SER B  211  GLU B  220  1                                  10    
HELIX   21  21 GLU B  221  SER B  233  1                                  13    
HELIX   22  22 ALA B  244  ARG B  251  1                                   8    
HELIX   23  23 PRO B  254  ASN B  264  1                                  11    
HELIX   24  24 GLN B  291  ILE B  298  5                                   8    
HELIX   25  25 GLY B  307  SER B  309  5                                   3    
HELIX   26  26 LYS B  310  PHE B  318  1                                   9    
HELIX   27  27 GLU B  330  ARG B  338  1                                   9    
SHEET    1   A 7 ASP A 109  VAL A 113  0                                        
SHEET    2   A 7 VAL A 325  ASP A 329  1  O  LEU A 326   N  ILE A 111           
SHEET    3   A 7 ASP A 300  VAL A 304  1  N  ALA A 303   O  VAL A 327           
SHEET    4   A 7 MET A 236  HIS A 239  1  N  LEU A 237   O  ILE A 302           
SHEET    5   A 7 LYS A 142  VAL A 147  1  N  ALA A 146   O  MET A 236           
SHEET    6   A 7 GLU A 168  PRO A 173  1  O  LEU A 170   N  VAL A 145           
SHEET    7   A 7 THR A 200  TYR A 201  1  O  THR A 200   N  PHE A 171           
SHEET    1   B 4 GLY A 242  GLU A 243  0                                        
SHEET    2   B 4 THR A 268  ALA A 270 -1  O  GLU A 269   N  GLY A 242           
SHEET    3   B 4 TYR A 273  PHE A 275 -1  O  PHE A 275   N  THR A 268           
SHEET    4   B 4 VAL A 281  LYS A 284 -1  O  HIS A 283   N  TYR A 274           
SHEET    1   C 7 ASP B 109  VAL B 113  0                                        
SHEET    2   C 7 THR B 324  ASP B 329  1  O  LEU B 326   N  ILE B 111           
SHEET    3   C 7 ASP B 300  VAL B 304  1  N  ALA B 303   O  VAL B 325           
SHEET    4   C 7 MET B 236  HIS B 239  1  N  LEU B 237   O  ILE B 302           
SHEET    5   C 7 LYS B 142  VAL B 147  1  N  ALA B 146   O  MET B 236           
SHEET    6   C 7 GLU B 168  PRO B 173  1  O  LEU B 170   N  VAL B 145           
SHEET    7   C 7 THR B 200  TYR B 201  1  O  THR B 200   N  LEU B 169           
SHEET    1   D 4 GLY B 242  GLU B 243  0                                        
SHEET    2   D 4 THR B 268  ALA B 270 -1  O  GLU B 269   N  GLY B 242           
SHEET    3   D 4 TYR B 273  PHE B 275 -1  O  PHE B 275   N  THR B 268           
SHEET    4   D 4 VAL B 281  LYS B 284 -1  O  HIS B 283   N  TYR B 274           
CISPEP   1 GLY A  208    GLN A  209          0       -14.46                     
SITE     1 AC1 10 GLY A 149  GLY A 150  THR A 151  THR A 152                    
SITE     2 AC1 10 GLY A 240  MET A 247  ARG A 250  ARG A 251                    
SITE     3 AC1 10 GLU A 269  LYS A 310                                          
SITE     1 AC2  9 GLY B 149  GLY B 150  THR B 151  THR B 152                    
SITE     2 AC2  9 MET B 247  ARG B 250  ARG B 251  GLU B 269                    
SITE     3 AC2  9 LYS B 310                                                     
CRYST1   55.537   83.822  113.712  90.00  90.00  90.00 P 21 21 21    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      0.018006  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011930  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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