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Database: PDB
Entry: 3BXG
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HEADER    GENE REGULATION                         13-JAN-08   3BXG              
TITLE     CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC    
TITLE    2 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN COMPLEX WITH GLUCOSE-
TITLE    3 6-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   7   29-JUL-20 3BXG    1       COMPND REMARK SEQADV HETNAM              
REVDAT   7 2                   1       SITE                                     
REVDAT   6   13-JUL-11 3BXG    1       VERSN                                    
REVDAT   5   09-JUN-09 3BXG    1       REVDAT                                   
REVDAT   4   24-FEB-09 3BXG    1       VERSN                                    
REVDAT   3   06-JAN-09 3BXG    1       JRNL                                     
REVDAT   2   19-AUG-08 3BXG    1       JRNL                                     
REVDAT   1   01-JUL-08 3BXG    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,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 46.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 46775                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2507                            
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) : 3005                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 185                          
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3777                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 487                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.30000                                             
REMARK   3    B33 (A**2) : 0.44000                                              
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): 0.129         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.132         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.236         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4030 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5475 ; 1.447 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   552 ; 7.640 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;37.316 ;25.394       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   754 ;12.821 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;12.978 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   639 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2973 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2018 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2805 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   439 ; 0.161 ; 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):    79 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    34 ; 0.160 ; 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):  2664 ; 0.690 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4153 ; 1.012 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1518 ; 1.919 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1299 ; 3.068 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     93       A     339      4                      
REMARK   3           1     B     89       B     338      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1147 ;  0.69 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1147 ;  1.09 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
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   126                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.5474  74.3632  76.7147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1464 T22:  -0.1152                                     
REMARK   3      T33:  -0.1399 T12:  -0.0033                                     
REMARK   3      T13:  -0.0135 T23:   0.0443                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0402 L22:   5.1573                                     
REMARK   3      L33:   4.7118 L12:   0.5882                                     
REMARK   3      L13:   0.4049 L23:   2.8596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0319 S12:  -0.2527 S13:  -0.2480                       
REMARK   3      S21:   0.1137 S22:  -0.0389 S23:  -0.0718                       
REMARK   3      S31:   0.1405 S32:  -0.0343 S33:   0.0070                       
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   127        A   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1045  78.0559  73.3615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1273 T22:  -0.0878                                     
REMARK   3      T33:  -0.1660 T12:  -0.0156                                     
REMARK   3      T13:  -0.0079 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4186 L22:   6.4257                                     
REMARK   3      L33:   3.0795 L12:  -5.1109                                     
REMARK   3      L13:  -2.1891 L23:   1.3865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1155 S12:  -0.2033 S13:   0.0303                       
REMARK   3      S21:   0.2055 S22:   0.2178 S23:   0.1657                       
REMARK   3      S31:   0.0789 S32:  -0.2464 S33:  -0.1023                       
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   144        A   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9174  77.3126  64.4515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0811 T22:  -0.1089                                     
REMARK   3      T33:  -0.1569 T12:  -0.0165                                     
REMARK   3      T13:  -0.0381 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5936 L22:   3.5456                                     
REMARK   3      L33:   2.2659 L12:  -1.2792                                     
REMARK   3      L13:  -0.1684 L23:  -0.0300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0218 S12:   0.2049 S13:  -0.2709                       
REMARK   3      S21:  -0.1065 S22:   0.0549 S23:   0.2215                       
REMARK   3      S31:   0.2238 S32:  -0.2161 S33:  -0.0766                       
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   165        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7545  82.8249  59.8735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0791 T22:  -0.0956                                     
REMARK   3      T33:  -0.1674 T12:   0.0057                                     
REMARK   3      T13:  -0.0407 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0466 L22:   3.2681                                     
REMARK   3      L33:   3.9651 L12:   0.7913                                     
REMARK   3      L13:  -0.1586 L23:  -0.6806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0240 S12:   0.3317 S13:  -0.0934                       
REMARK   3      S21:  -0.1582 S22:   0.0688 S23:   0.1457                       
REMARK   3      S31:  -0.0576 S32:  -0.0435 S33:  -0.0449                       
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   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0758  98.7955  49.7082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2190 T22:   0.2496                                     
REMARK   3      T33:   0.3519 T12:  -0.0116                                     
REMARK   3      T13:  -0.0119 T23:   0.1292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5891 L22:  25.3016                                     
REMARK   3      L33:  17.0738 L12:   7.5895                                     
REMARK   3      L13:  -5.4763 L23: -20.1480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6732 S12:  -0.5836 S13:  -0.4318                       
REMARK   3      S21:  -0.8781 S22:  -0.5637 S23:  -2.3494                       
REMARK   3      S31:  -0.1052 S32:   1.3771 S33:   1.2369                       
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   221        A   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7037  93.9579  63.0340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0135 T22:  -0.0998                                     
REMARK   3      T33:  -0.0708 T12:   0.0168                                     
REMARK   3      T13:  -0.0510 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0751 L22:   3.7474                                     
REMARK   3      L33:   3.8310 L12:  -1.8097                                     
REMARK   3      L13:   0.9210 L23:  -1.0611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1493 S12:   0.1569 S13:   0.4145                       
REMARK   3      S21:  -0.0672 S22:   0.0644 S23:   0.2417                       
REMARK   3      S31:  -0.6224 S32:  -0.2912 S33:   0.0849                       
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   241        A   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  78.2680  89.0042  56.8468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0100 T22:  -0.0051                                     
REMARK   3      T33:  -0.0932 T12:  -0.0581                                     
REMARK   3      T13:   0.0558 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.0350 L22:  11.9924                                     
REMARK   3      L33:  10.9234 L12:  10.6271                                     
REMARK   3      L13:  -9.0897 L23:  -8.2265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5712 S12:   0.5556 S13:  -0.1312                       
REMARK   3      S21:  -1.0923 S22:   0.4422 S23:  -0.4317                       
REMARK   3      S31:   0.4318 S32:  -0.3091 S33:   0.1290                       
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   261        A   285                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.6018  92.8277  65.6416              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0525 T22:  -0.0815                                     
REMARK   3      T33:  -0.1413 T12:  -0.0701                                     
REMARK   3      T13:  -0.0092 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9424 L22:   4.7100                                     
REMARK   3      L33:   4.8740 L12:   0.8646                                     
REMARK   3      L13:  -0.4957 L23:  -1.6533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1652 S12:   0.3136 S13:   0.1222                       
REMARK   3      S21:  -0.1791 S22:   0.0631 S23:  -0.1541                       
REMARK   3      S31:  -0.4735 S32:   0.2673 S33:   0.1021                       
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   286        A   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.4475  86.6504  71.3647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1161 T22:  -0.1128                                     
REMARK   3      T33:  -0.1802 T12:  -0.0425                                     
REMARK   3      T13:  -0.0026 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2437 L22:   2.6104                                     
REMARK   3      L33:   1.9311 L12:  -0.0410                                     
REMARK   3      L13:   0.5766 L23:  -0.0572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0558 S12:   0.0363 S13:   0.2663                       
REMARK   3      S21:   0.0451 S22:  -0.0044 S23:  -0.0082                       
REMARK   3      S31:  -0.2579 S32:   0.1296 S33:   0.0602                       
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   334        A   339                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.3630  74.2592  78.3475              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1209 T22:  -0.0731                                     
REMARK   3      T33:  -0.1171 T12:  -0.0074                                     
REMARK   3      T13:  -0.0286 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.3892 L22:  22.3953                                     
REMARK   3      L33:  24.5448 L12:  -0.0293                                     
REMARK   3      L13:  17.2396 L23:   3.7436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4422 S12:   0.1209 S13:  -0.6023                       
REMARK   3      S21:   0.6413 S22:   0.1528 S23:  -1.1386                       
REMARK   3      S31:   0.5997 S32:  -0.2378 S33:  -0.5950                       
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   120        B   178                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6245  74.2635  37.6639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1217 T22:  -0.1392                                     
REMARK   3      T33:  -0.1326 T12:   0.0001                                     
REMARK   3      T13:  -0.0197 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5941 L22:   2.5032                                     
REMARK   3      L33:   1.9477 L12:   0.9867                                     
REMARK   3      L13:  -0.6627 L23:  -0.5219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0754 S12:  -0.0762 S13:  -0.2213                       
REMARK   3      S21:   0.0074 S22:   0.0186 S23:  -0.1811                       
REMARK   3      S31:   0.1279 S32:   0.0790 S33:   0.0568                       
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   179        B   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4506  81.4841  44.7413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0742 T22:  -0.0604                                     
REMARK   3      T33:  -0.1634 T12:  -0.0269                                     
REMARK   3      T13:  -0.0400 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2375 L22:   5.6640                                     
REMARK   3      L33:   5.1543 L12:  -3.8873                                     
REMARK   3      L13:  -2.7847 L23:   3.6770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0022 S12:  -0.3558 S13:  -0.0134                       
REMARK   3      S21:   0.3266 S22:   0.0680 S23:  -0.2170                       
REMARK   3      S31:  -0.0130 S32:   0.0011 S33:  -0.0702                       
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   203        B   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1623 100.8852  42.4641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1996 T22:  -0.0047                                     
REMARK   3      T33:  -0.0459 T12:   0.0572                                     
REMARK   3      T13:   0.0104 T23:  -0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9170 L22:  18.2036                                     
REMARK   3      L33:   4.0744 L12:  -9.0476                                     
REMARK   3      L13:  -3.9221 L23:   8.4300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0676 S12:   0.1637 S13:   0.1354                       
REMARK   3      S21:   0.2339 S22:   0.0162 S23:   0.1332                       
REMARK   3      S31:  -0.3661 S32:  -0.3742 S33:  -0.0838                       
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   222        B   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4687  88.3207  33.6126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0960 T22:  -0.1394                                     
REMARK   3      T33:  -0.1525 T12:   0.0150                                     
REMARK   3      T13:   0.0166 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2498 L22:   2.2049                                     
REMARK   3      L33:   1.6511 L12:   0.4828                                     
REMARK   3      L13:  -1.3146 L23:   0.2753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.0167 S13:   0.2299                       
REMARK   3      S21:  -0.0835 S22:   0.0929 S23:  -0.2806                       
REMARK   3      S31:  -0.1862 S32:   0.1002 S33:  -0.1032                       
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   243        B   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8860  93.9507  47.8638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1573 T22:  -0.0416                                     
REMARK   3      T33:  -0.0608 T12:   0.0175                                     
REMARK   3      T13:   0.1005 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8618 L22:  15.3002                                     
REMARK   3      L33:   7.7292 L12:  -4.9596                                     
REMARK   3      L13:  -1.2064 L23:   4.3354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0710 S12:  -0.2497 S13:   0.5037                       
REMARK   3      S21:   1.2630 S22:   0.2965 S23:  -0.4485                       
REMARK   3      S31:  -0.3465 S32:   0.4497 S33:  -0.2256                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   261        B   285                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9788  92.1661  37.8756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0585 T22:  -0.1206                                     
REMARK   3      T33:  -0.1158 T12:   0.0479                                     
REMARK   3      T13:   0.0330 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4457 L22:   5.7344                                     
REMARK   3      L33:   4.6971 L12:  -0.0393                                     
REMARK   3      L13:   0.2590 L23:  -0.9800                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0177 S12:  -0.0080 S13:   0.2108                       
REMARK   3      S21:   0.2421 S22:   0.1418 S23:   0.1684                       
REMARK   3      S31:  -0.4641 S32:  -0.1743 S33:  -0.1242                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   286        B   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2681  92.9066  31.8642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0800 T22:  -0.0762                                     
REMARK   3      T33:  -0.0468 T12:   0.0146                                     
REMARK   3      T13:   0.0217 T23:   0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0698 L22:  14.3483                                     
REMARK   3      L33:  20.4387 L12:   1.7990                                     
REMARK   3      L13:   1.0977 L23:  15.6930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1621 S12:   0.2339 S13:   0.5854                       
REMARK   3      S21:  -0.4428 S22:  -0.2451 S23:   0.1582                       
REMARK   3      S31:  -0.8640 S32:  -0.5405 S33:   0.0830                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   297        B   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.7541  78.5610  34.0282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1337 T22:  -0.1282                                     
REMARK   3      T33:  -0.1397 T12:   0.0014                                     
REMARK   3      T13:   0.0035 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2273 L22:   2.6832                                     
REMARK   3      L33:   2.6385 L12:   0.6184                                     
REMARK   3      L13:  -0.5347 L23:  -1.2169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:   0.1182 S13:  -0.0660                       
REMARK   3      S21:  -0.0290 S22:   0.0520 S23:   0.2332                       
REMARK   3      S31:  -0.0544 S32:  -0.1818 S33:  -0.0502                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BXG 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 DEPOSITION ID IS D_1000046077.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-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) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK HIGH-RESOLUTION     
REMARK 200                                   DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49657                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.1000                            
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     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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   (%): 48.66                                     
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 GLUCOSE-6-       
REMARK 280  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       27.74700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.79150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.90300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.79150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.74700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.90300            
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     GLU A   340                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     GLU B   340                                                      
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   CD1  ILE A   111     SG   CYS A   134              1.69            
REMARK 500   O    GLY A   176     O    HOH A   570              2.04            
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    GLN A 209   CD    GLN A 209   NE2     0.181                       
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    SER A 120   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    GLY B 176   N   -  CA  -  C   ANGL. DEV. =  19.9 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    SER A 120       72.08   -162.26                                   
REMARK 500    GLN A 209      -16.91     81.67                                   
REMARK 500    PHE A 271       41.94     39.95                                   
REMARK 500    SER B 140     -164.50   -107.47                                   
REMARK 500    SER B 140     -162.16   -110.51                                   
REMARK 500    LEU B 178       11.74     58.38                                   
REMARK 500    SER B 287      141.28   -172.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  119     SER A  120                 -121.12                    
REMARK 500 ARG B  175     GLY B  176                  119.96                    
REMARK 500 GLY B  176     GLY B  177                 -145.77                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OKG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC   
REMARK 900 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS                         
REMARK 900 RELATED ID: 3BXE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC   
REMARK 900 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN COMPLEX WITH         
REMARK 900 DIHYDROXYACETONE PHOSPHATE                                           
REMARK 900 RELATED ID: 3BXF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC   
REMARK 900 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN COMPLEX WITH         
REMARK 900 EFFECTOR FRUCTOSE-1,6-BISPHOSPHATE                                   
REMARK 900 RELATED ID: 3BXH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EFFECTOR BINDING DOMAIN OF CENTRAL GLYCOLYTIC   
REMARK 900 GENE REGULATOR (CGGR) FROM BACILLUS SUBTILIS IN COMPLEX WITH         
REMARK 900 FRUCTOSE-6-PHOSPHATE                                                 
DBREF  3BXG A   89   340  UNP    O32253   CGGR_BACSU      89    340             
DBREF  3BXG B   89   340  UNP    O32253   CGGR_BACSU      89    340             
SEQADV 3BXG SER A   86  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXG ASN A   87  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXG ALA A   88  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXG SER B   86  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXG ASN B   87  UNP  O32253              EXPRESSION TAG                 
SEQADV 3BXG 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    BG6  A 401      16                                                       
HET    BG6  B 401      16                                                       
HETNAM     BG6 6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE                               
FORMUL   3  BG6    2(C6 H13 O9 P)                                               
FORMUL   5  HOH   *487(H2 O)                                                    
HELIX    1   1 THR A   95  ASN A  106  1                                  12    
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  SER A  198  1                                  14    
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  LEU A  337  1                                   8    
HELIX   14  14 SER B   86  ALA B   88  1                                   3    
HELIX   15  15 LYS B   89  LEU B   92  1                                   4    
HELIX   16  16 GLY B   93  ASN B  106  1                                  14    
HELIX   17  17 SER B  120  PHE B  139  1                                  20    
HELIX   18  18 GLY B  150  MET B  160  1                                  11    
HELIX   19  19 ASP B  181  ASN B  184  5                                   4    
HELIX   20  20 GLN B  185  SER B  198  1                                  14    
HELIX   21  21 SER B  211  GLU B  220  1                                  10    
HELIX   22  22 GLU B  221  SER B  233  1                                  13    
HELIX   23  23 ALA B  244  ARG B  251  1                                   8    
HELIX   24  24 PRO B  254  ASN B  264  1                                  11    
HELIX   25  25 GLN B  291  ILE B  298  5                                   8    
HELIX   26  26 GLY B  307  SER B  309  5                                   3    
HELIX   27  27 LYS B  310  PHE B  318  1                                   9    
HELIX   28  28 GLU B  330  ARG B  338  1                                   9    
SHEET    1   A 7 ASP A 109  VAL A 113  0                                        
SHEET    2   A 7 THR A 324  ASP A 329  1  O  THR A 328   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  VAL A 282   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 327           
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 PRO A  207    GLY A  208          0        13.08                     
CRYST1   55.494   83.806  113.583  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      0.018020  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011932  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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