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Database: PDB
Entry: 6FPL
LinkDB: 6FPL
Original site: 6FPL 
HEADER    TRANSCRIPTION                           11-FEB-18   6FPL              
TITLE     TETR(D) E147A MUTANT IN COMPLEX WITH TETRACYCLINE AND MAGNESIUM       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TETRACYCLINE REPRESSOR PROTEIN CLASS D;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: STOP CODON AT 209, C-TERMINUS REMOVED FOR BETTER      
COMPND   7 CRYSTALLIZATION                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: TETR;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PWH1950                                   
KEYWDS    TRANSCRIPTION REGULATION, TRANSCRIPTION                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.HINRICHS,G.J.PALM,L.BERNDT,B.GIRBARDT                               
REVDAT   3   17-JAN-24 6FPL    1       REMARK LINK                              
REVDAT   2   18-MAR-20 6FPL    1       JRNL                                     
REVDAT   1   13-MAR-19 6FPL    0                                                
JRNL        AUTH   G.J.PALM,I.BUCHHOLZ,S.WERTEN,B.GIRBARDT,L.BERNDT,M.DELCEA,   
JRNL        AUTH 2 W.HINRICHS                                                   
JRNL        TITL   THERMODYNAMICS, COOPERATIVITY AND STABILITY OF THE           
JRNL        TITL 2 TETRACYCLINE REPRESSOR (TETR) UPON TETRACYCLINE BINDING.     
JRNL        REF    BIOCHIM BIOPHYS ACTA          V.1868 40404 2020              
JRNL        REF  2 PROTEINS PROTEOM                                             
JRNL        REFN                   ISSN 1878-1454                               
JRNL        PMID   32114262                                                     
JRNL        DOI    10.1016/J.BBAPAP.2020.140404                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.WERTEN,J.SCHNEIDER,G.J.PALM,W.HINRICHS                     
REMARK   1  TITL   MODULAR ORGANISATION OF INDUCER RECOGNITION AND ALLOSTERY IN 
REMARK   1  TITL 2 THE TETRACYCLINE REPRESSOR.                                  
REMARK   1  REF    FEBS J.                       V. 283  2102 2016              
REMARK   1  REFN                   ISSN 1742-4658                               
REMARK   1  PMID   27028290                                                     
REMARK   1  DOI    10.1111/FEBS.13723                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25266                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1318                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1862                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1570                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 95                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.65000                                              
REMARK   3    B22 (A**2) : 1.65000                                              
REMARK   3    B33 (A**2) : -3.30000                                             
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): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.638         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1677 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1625 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2287 ; 1.837 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3709 ; 0.939 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   206 ; 5.196 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;37.058 ;23.457       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   289 ;13.727 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   259 ; 0.146 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1941 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   407 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   815 ; 1.987 ; 2.386       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   814 ; 1.981 ; 2.386       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1024 ; 2.647 ; 3.569       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1025 ; 2.646 ; 3.569       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   861 ; 2.904 ; 2.674       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   862 ; 2.903 ; 2.674       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1264 ; 4.275 ; 3.903       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2030 ; 5.226 ;19.550       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1998 ; 5.182 ;19.411       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    45                          
REMARK   3    RESIDUE RANGE :   A    46        A    64                          
REMARK   3    RESIDUE RANGE :   A  1212        A  1216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9450  28.4028  13.5477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0839 T22:   0.1270                                     
REMARK   3      T33:   0.1150 T12:  -0.0335                                     
REMARK   3      T13:  -0.0336 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1642 L22:   0.6879                                     
REMARK   3      L33:   3.7222 L12:  -0.6965                                     
REMARK   3      L13:   2.4130 L23:  -0.0900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0063 S12:   0.0536 S13:   0.0397                       
REMARK   3      S21:   0.1149 S22:   0.0562 S23:  -0.0818                       
REMARK   3      S31:   0.1945 S32:   0.1222 S33:  -0.0624                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 7                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    65        A    93                          
REMARK   3    RESIDUE RANGE :   A   101        A   106                          
REMARK   3    RESIDUE RANGE :   A   107        A   123                          
REMARK   3    RESIDUE RANGE :   A    94        A   100                          
REMARK   3    RESIDUE RANGE :   A   124        A   155                          
REMARK   3    RESIDUE RANGE :   A   182        A   208                          
REMARK   3    RESIDUE RANGE :   A  1209        A  1211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9475  32.4410  39.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1312 T22:   0.0812                                     
REMARK   3      T33:   0.1225 T12:   0.0989                                     
REMARK   3      T13:  -0.0196 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6441 L22:   0.1503                                     
REMARK   3      L33:   1.1570 L12:   0.2718                                     
REMARK   3      L13:   0.0031 L23:   0.1602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0151 S12:   0.0454 S13:   0.0185                       
REMARK   3      S21:  -0.0005 S22:   0.0093 S23:   0.0448                       
REMARK   3      S31:   0.0351 S32:  -0.0450 S33:  -0.0244                       
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   165        A   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5302  20.5510  35.6989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3470 T22:   0.1404                                     
REMARK   3      T33:   0.1830 T12:   0.2007                                     
REMARK   3      T13:   0.0719 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9460 L22:   2.8582                                     
REMARK   3      L33:   0.6175 L12:   3.7540                                     
REMARK   3      L13:   1.7323 L23:   1.3126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0268 S12:   0.1648 S13:  -0.4925                       
REMARK   3      S21:  -0.0880 S22:   0.1334 S23:  -0.3586                       
REMARK   3      S31:   0.0290 S32:   0.0824 S33:  -0.1066                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008642.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.602                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 17.66                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.9500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2TRT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT 0.1M NA-CITRAT, 0.8M         
REMARK 280  LI2SO4, 0.5M (NH4)2SO4, 0.1ML PROTEIN (10.19MG/ML, 0.1M MES PH      
REMARK 280  6.5) + 0.1ML 2MM TC + 0.001ML 3M MGCL2 1:4 PRECIPITANT/PROTEIN,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       34.01000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       34.01000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.51500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.75750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       34.01000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      134.27250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      134.27250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.01000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       44.75750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       34.01000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.51500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       34.01000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       89.51500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       34.01000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      134.27250            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       44.75750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       34.01000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       44.75750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      134.27250            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       34.01000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       34.01000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       89.51500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       68.02000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       68.02000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 429  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 495  LIES ON A SPECIAL POSITION.                          
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     THR A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     PRO A   162                                                      
REMARK 465     ASP A   163                                                      
REMARK 465     GLU A   164                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  107   CB   CG   CD   OE1  OE2                             
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   O    HOH A   409     O    HOH A   484              2.11            
REMARK 500   OE1  GLU A    58     O    HOH A   401              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN A    32     OE1  GLN A    32    15555     2.06            
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    LEU A  41   CB  -  CG  -  CD2 ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG A 171   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A 171   NE  -  CZ  -  NH2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  66       63.76   -102.28                                   
REMARK 500    LEU A 204     -123.11     51.32                                   
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 495        DISTANCE =  6.00 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TAC A 301   O11                                                    
REMARK 620 2 TAC A 301   O12  86.4                                              
REMARK 620 3 HOH A 421   O    93.2 178.6                                        
REMARK 620 4 HOH A 439   O    93.7  91.3  87.4                                  
REMARK 620 5 HOH A 457   O    86.9  94.0  87.3 174.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TAC A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 308                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2TRT   RELATED DB: PDB                                   
REMARK 900 TETR(D) TETRACYCLINE COMPLEX                                         
REMARK 900 RELATED ID: 2TCT   RELATED DB: PDB                                   
REMARK 900 TETR(D) 7-CHLORTETRACYCLINE COMPLEX                                  
DBREF  6FPL A    2   208  UNP    P0ACT4   TETR4_ECOLX      2    208             
SEQADV 6FPL SER A    2  UNP  P0ACT4    ALA     2 ENGINEERED MUTATION            
SEQADV 6FPL ALA A  147  UNP  P0ACT4    GLU   147 ENGINEERED MUTATION            
SEQRES   1 A  207  SER ARG LEU ASN ARG GLU SER VAL ILE ASP ALA ALA LEU          
SEQRES   2 A  207  GLU LEU LEU ASN GLU THR GLY ILE ASP GLY LEU THR THR          
SEQRES   3 A  207  ARG LYS LEU ALA GLN LYS LEU GLY ILE GLU GLN PRO THR          
SEQRES   4 A  207  LEU TYR TRP HIS VAL LYS ASN LYS ARG ALA LEU LEU ASP          
SEQRES   5 A  207  ALA LEU ALA VAL GLU ILE LEU ALA ARG HIS HIS ASP TYR          
SEQRES   6 A  207  SER LEU PRO ALA ALA GLY GLU SER TRP GLN SER PHE LEU          
SEQRES   7 A  207  ARG ASN ASN ALA MET SER PHE ARG ARG ALA LEU LEU ARG          
SEQRES   8 A  207  TYR ARG ASP GLY ALA LYS VAL HIS LEU GLY THR ARG PRO          
SEQRES   9 A  207  ASP GLU LYS GLN TYR ASP THR VAL GLU THR GLN LEU ARG          
SEQRES  10 A  207  PHE MET THR GLU ASN GLY PHE SER LEU ARG ASP GLY LEU          
SEQRES  11 A  207  TYR ALA ILE SER ALA VAL SER HIS PHE THR LEU GLY ALA          
SEQRES  12 A  207  VAL LEU ALA GLN GLN GLU HIS THR ALA ALA LEU THR ASP          
SEQRES  13 A  207  ARG PRO ALA ALA PRO ASP GLU ASN LEU PRO PRO LEU LEU          
SEQRES  14 A  207  ARG GLU ALA LEU GLN ILE MET ASP SER ASP ASP GLY GLU          
SEQRES  15 A  207  GLN ALA PHE LEU HIS GLY LEU GLU SER LEU ILE ARG GLY          
SEQRES  16 A  207  PHE GLU VAL GLN LEU THR ALA LEU LEU GLN ILE VAL              
HET    TAC  A 301      32                                                       
HET     MG  A 302       1                                                       
HET     CL  A 303       1                                                       
HET     CL  A 304       1                                                       
HET     CL  A 305       1                                                       
HET     CL  A 306       1                                                       
HET     CL  A 307       1                                                       
HET     CL  A 308       1                                                       
HETNAM     TAC TETRACYCLINE                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  TAC    C22 H24 N2 O8                                                
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   CL    6(CL 1-)                                                     
FORMUL  10  HOH   *95(H2 O)                                                     
HELIX    1 AA1 ASN A    5  GLY A   21  1                                  17    
HELIX    2 AA2 THR A   26  GLY A   35  1                                  10    
HELIX    3 AA3 GLU A   37  VAL A   45  1                                   9    
HELIX    4 AA4 ASN A   47  HIS A   64  1                                  18    
HELIX    5 AA5 SER A   74  ARG A   92  1                                  19    
HELIX    6 AA6 ASP A   95  LEU A  101  1                                   7    
HELIX    7 AA7 ASP A  106  LYS A  108  5                                   3    
HELIX    8 AA8 GLN A  109  ASN A  123  1                                  15    
HELIX    9 AA9 SER A  126  LEU A  155  1                                  30    
HELIX   10 AB1 PRO A  167  ASP A  180  1                                  14    
HELIX   11 AB2 GLY A  182  LEU A  204  1                                  23    
LINK         O11 TAC A 301                MG    MG A 302     1555   1555  2.00  
LINK         O12 TAC A 301                MG    MG A 302     1555   1555  1.90  
LINK        MG    MG A 302                 O   HOH A 421     1555   1555  2.13  
LINK        MG    MG A 302                 O   HOH A 439     1555   1555  2.03  
LINK        MG    MG A 302                 O   HOH A 457     1555   1555  2.19  
SITE     1 AC1 17 HIS A  64  SER A  67  ASN A  82  PHE A  86                    
SITE     2 AC1 17 HIS A 100  ARG A 104  PRO A 105  VAL A 113                    
SITE     3 AC1 17 GLN A 116  ILE A 134  SER A 138  MET A 177                    
SITE     4 AC1 17  MG A 302  HOH A 421  HOH A 439  HOH A 445                    
SITE     5 AC1 17 HOH A 457                                                     
SITE     1 AC2  5 HIS A 100  TAC A 301  HOH A 421  HOH A 439                    
SITE     2 AC2  5 HOH A 457                                                     
SITE     1 AC3  2 GLY A 102  HOH A 421                                          
SITE     1 AC4  5 ARG A   3  LEU A   4  GLN A  76  ARG A  80                    
SITE     2 AC4  5 HOH A 446                                                     
SITE     1 AC5  3 ASN A   5  ARG A   6  GLU A   7                               
SITE     1 AC6  2 THR A  26  THR A  27                                          
SITE     1 AC7  4 SER A   2  ARG A   3  SER A  74  SER A  77                    
SITE     1 AC8  1 THR A  26                                                     
CRYST1   68.020   68.020  179.030  90.00  90.00  90.00 I 41 2 2     16          
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      0.014702  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005586        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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