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Database: PDB
Entry: 3TQT
LinkDB: 3TQT
Original site: 3TQT 
HEADER    LIGASE                                  09-SEP-11   3TQT              
TITLE     STRUCTURE OF THE D-ALANINE-D-ALANINE LIGASE FROM COXIELLA BURNETII    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: COXIELLA BURNETII;                              
SOURCE   3 ORGANISM_TAXID: 227377;                                              
SOURCE   4 STRAIN: RSA493;                                                      
SOURCE   5 GENE: DDL, CBU_1338;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    CELL ENVELOPE, LIGASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RUDOLPH,J.CHEUNG,M.FRANKLIN,M.CASSIDY,E.GARY,F.BURSHTEYN,J.LOVE     
REVDAT   1   28-SEP-11 3TQT    0                                                
JRNL        AUTH   M.RUDOLPH,J.CHEUNG,M.FRANKLIN,M.CASSIDY,E.GARY,F.BURSHTEYN,  
JRNL        AUTH 2 J.LOVE                                                       
JRNL        TITL   STRUCTURE OF THE D-ALANINE-D-ALANINE LIGASE FROM COXIELLA    
JRNL        TITL 2 BURNETII                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 56794                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2875                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.6603 -  4.0441    0.97     5668   282  0.1712 0.1859        
REMARK   3     2  4.0441 -  3.2104    0.99     5593   311  0.1681 0.2116        
REMARK   3     3  3.2104 -  2.8047    0.99     5559   283  0.1873 0.2371        
REMARK   3     4  2.8047 -  2.5483    0.99     5524   291  0.1981 0.2338        
REMARK   3     5  2.5483 -  2.3657    0.99     5453   315  0.1898 0.2488        
REMARK   3     6  2.3657 -  2.2262    0.99     5469   280  0.1825 0.2480        
REMARK   3     7  2.2262 -  2.1148    0.98     5404   298  0.1798 0.2465        
REMARK   3     8  2.1148 -  2.0227    0.97     5348   291  0.1834 0.2473        
REMARK   3     9  2.0227 -  1.9448    0.96     5306   283  0.1900 0.2526        
REMARK   3    10  1.9448 -  1.8800    0.83     4595   241  0.2186 0.2892        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 41.04                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.83710                                              
REMARK   3    B22 (A**2) : -6.02470                                             
REMARK   3    B33 (A**2) : 3.18760                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5442                                  
REMARK   3   ANGLE     :  1.055           7379                                  
REMARK   3   CHIRALITY :  0.068            856                                  
REMARK   3   PLANARITY :  0.005            942                                  
REMARK   3   DIHEDRAL  : 14.269           2011                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 2:132)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  64.1891  62.5449  -8.4817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2503 T22:   0.1562                                     
REMARK   3      T33:   0.1986 T12:  -0.0587                                     
REMARK   3      T13:  -0.0792 T23:   0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0631 L22:   0.7483                                     
REMARK   3      L33:   1.6763 L12:  -0.5555                                     
REMARK   3      L13:  -0.0945 L23:  -0.0181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0997 S12:  -0.0943 S13:  -0.1230                       
REMARK   3      S21:   0.2549 S22:  -0.0389 S23:   0.0340                       
REMARK   3      S31:   0.0270 S32:  -0.0780 S33:  -0.0436                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 133:172)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  53.6017  43.6705 -32.7004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1875 T22:   0.1735                                     
REMARK   3      T33:   0.1847 T12:   0.0038                                     
REMARK   3      T13:  -0.0279 T23:  -0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6804 L22:   0.5175                                     
REMARK   3      L33:   0.1403 L12:  -0.0493                                     
REMARK   3      L13:   0.0089 L23:  -0.2758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0644 S12:   0.0549 S13:  -0.2601                       
REMARK   3      S21:  -0.0566 S22:  -0.1508 S23:   0.0093                       
REMARK   3      S31:   0.0211 S32:  -0.0469 S33:   0.0293                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 173:224)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  53.0146  34.2665 -26.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2226 T22:   0.1736                                     
REMARK   3      T33:   0.3568 T12:  -0.0150                                     
REMARK   3      T13:  -0.0294 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8636 L22:   0.5701                                     
REMARK   3      L33:   0.8777 L12:  -0.0519                                     
REMARK   3      L13:  -0.1077 L23:   0.1131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.0347 S13:  -0.5365                       
REMARK   3      S21:   0.1841 S22:  -0.1693 S23:  -0.1399                       
REMARK   3      S31:   0.0936 S32:  -0.0097 S33:   0.0471                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 225:355)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3767  50.2066 -27.9039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1660 T22:   0.1773                                     
REMARK   3      T33:   0.2667 T12:   0.0061                                     
REMARK   3      T13:  -0.0305 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7125 L22:   1.6164                                     
REMARK   3      L33:   0.9713 L12:  -0.2843                                     
REMARK   3      L13:  -0.1439 L23:   0.3612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0004 S12:   0.0206 S13:  -0.1178                       
REMARK   3      S21:  -0.0377 S22:   0.0021 S23:  -0.4185                       
REMARK   3      S31:   0.0500 S32:   0.1131 S33:   0.0172                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 356:371)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6854  79.2236 -30.7631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2640 T22:   0.1982                                     
REMARK   3      T33:   0.2737 T12:   0.0181                                     
REMARK   3      T13:  -0.0306 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0132 L22:   0.7925                                     
REMARK   3      L33:   0.4658 L12:  -0.2803                                     
REMARK   3      L13:   0.1258 L23:  -0.1514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0247 S12:  -0.2827 S13:   0.6469                       
REMARK   3      S21:   0.2101 S22:  -0.0068 S23:  -0.2437                       
REMARK   3      S31:  -0.2061 S32:  -0.1300 S33:   0.0363                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain B and resid 4:99)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5108  73.6549 -13.5424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1890 T22:   0.2089                                     
REMARK   3      T33:   0.1867 T12:   0.0265                                     
REMARK   3      T13:   0.0436 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0151 L22:   2.5041                                     
REMARK   3      L33:   1.2722 L12:  -0.8335                                     
REMARK   3      L13:   0.0651 L23:   0.2884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0327 S12:  -0.0995 S13:   0.0973                       
REMARK   3      S21:   0.1734 S22:  -0.0030 S23:   0.0371                       
REMARK   3      S31:  -0.2094 S32:  -0.0514 S33:  -0.0181                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain B and resid 100:158)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7626  60.2825 -28.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1701 T22:   0.1928                                     
REMARK   3      T33:   0.1599 T12:   0.0361                                     
REMARK   3      T13:  -0.0382 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8619 L22:   1.1208                                     
REMARK   3      L33:   0.9233 L12:   0.0637                                     
REMARK   3      L13:  -0.3660 L23:   0.3961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1066 S12:   0.0102 S13:  -0.0251                       
REMARK   3      S21:  -0.1817 S22:  -0.0273 S23:   0.1130                       
REMARK   3      S31:  -0.3040 S32:   0.0967 S33:  -0.1130                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain B and resid 159:224)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  56.4284  70.1618 -47.4729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3374 T22:   0.3315                                     
REMARK   3      T33:   0.1439 T12:  -0.0165                                     
REMARK   3      T13:   0.0095 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3925 L22:   1.6706                                     
REMARK   3      L33:   0.6043 L12:   0.3384                                     
REMARK   3      L13:   0.1016 L23:  -0.0549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0621 S12:   0.5062 S13:   0.0532                       
REMARK   3      S21:  -0.5391 S22:   0.1263 S23:  -0.0833                       
REMARK   3      S31:  -0.1171 S32:   0.1184 S33:  -0.0620                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain B and resid 225:320)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8602  58.4658 -40.6552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3002 T22:   0.2648                                     
REMARK   3      T33:   0.2322 T12:   0.0417                                     
REMARK   3      T13:  -0.1419 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3238 L22:   1.5266                                     
REMARK   3      L33:   0.8477 L12:  -0.0380                                     
REMARK   3      L13:   0.5922 L23:   0.1612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0940 S12:   0.1942 S13:  -0.0863                       
REMARK   3      S21:  -0.3415 S22:   0.0437 S23:   0.3494                       
REMARK   3      S31:   0.0272 S32:   0.0457 S33:  -0.0214                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (chain B and resid 321:368)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0048  56.5621 -22.2608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1803 T22:   0.2024                                     
REMARK   3      T33:   0.2432 T12:  -0.0132                                     
REMARK   3      T13:  -0.0108 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5399 L22:   1.7522                                     
REMARK   3      L33:   1.3267 L12:   0.2538                                     
REMARK   3      L13:  -0.1824 L23:   0.1161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1103 S12:   0.0061 S13:  -0.1938                       
REMARK   3      S21:   0.0059 S22:  -0.0698 S23:   0.5438                       
REMARK   3      S31:   0.1663 S32:  -0.1844 S33:  -0.0225                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3TQT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067807.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : 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                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56853                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37900                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 5% PEG 3350, 30%      
REMARK 280  PEG 200, SITTING DROP, TEMPERATURE 293K                             
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       34.11900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.28150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.72100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.28150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.11900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.72100            
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 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: 4590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     ASP A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     HIS A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     TYR A   254                                                      
REMARK 465     TYR A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     TYR A   257                                                      
REMARK 465     ASP A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     TYR A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     ASN B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     HIS B   251                                                      
REMARK 465     HIS B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     TYR B   254                                                      
REMARK 465     TYR B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     TYR B   257                                                      
REMARK 465     ASP B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     LYS B   260                                                      
REMARK 465     TYR B   261                                                      
REMARK 465     LEU B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     PRO B   264                                                      
REMARK 465     ASN B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     SER B   272                                                      
REMARK 465     VAL B   273                                                      
REMARK 465     ASP B   274                                                      
REMARK 465     LEU B   275                                                      
REMARK 465     ALA B   369                                                      
REMARK 465     ARG B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     LEU B   372                                                      
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    THR A  77     -163.95   -125.83                                   
REMARK 500    GLN A 110      -43.42     74.94                                   
REMARK 500    ASN A 237      -93.25   -109.58                                   
REMARK 500    ALA A 239       73.58   -115.89                                   
REMARK 500    ASP A 274       69.17   -101.07                                   
REMARK 500    THR B  77     -167.37   -128.18                                   
REMARK 500    GLN B 110      -20.26     69.18                                   
REMARK 500    ASN B 237      -98.67   -110.49                                   
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 534        DISTANCE =  5.68 ANGSTROMS                       
DBREF  3TQT A    1   372  UNP    Q83BZ9   DDL_COXBU        1    372             
DBREF  3TQT B    1   372  UNP    Q83BZ9   DDL_COXBU        1    372             
SEQRES   1 A  372  MET ALA GLU LYS LEU HIS ILE SER VAL LEU CYS GLY GLY          
SEQRES   2 A  372  GLN SER THR GLU HIS GLU ILE SER ILE GLN SER ALA LYS          
SEQRES   3 A  372  ASN ILE VAL ASN THR LEU ASP ALA ALA LYS TYR LEU ILE          
SEQRES   4 A  372  SER VAL ILE PHE ILE ASP HIS VAL GLY ARG TRP TYR LEU          
SEQRES   5 A  372  ILE ASP GLN PRO GLU MET PHE LEU ALA HIS SER PRO ASP          
SEQRES   6 A  372  HIS LEU VAL LYS GLU GLY SER ALA ARG PRO ILE THR ILE          
SEQRES   7 A  372  ALA PHE GLY ASP ALA ALA LYS PRO TRP GLN SER LEU ASN          
SEQRES   8 A  372  GLY ASP GLY ARG ARG TYR SER ALA ASP CYS VAL PHE PRO          
SEQRES   9 A  372  MET VAL HIS GLY THR GLN GLY GLU ASP GLY ALA LEU GLN          
SEQRES  10 A  372  GLY LEU LEU GLU LEU LEU ASN LEU PRO TYR VAL GLY ALA          
SEQRES  11 A  372  ASN VAL GLN SER SER ALA VAL CYS MET GLU LYS ASP LEU          
SEQRES  12 A  372  THR LYS THR VAL LEU ARG ALA GLY GLY ILE PRO VAL VAL          
SEQRES  13 A  372  ASP TRP HIS THR LEU SER PRO ARG ASP ALA THR GLU GLY          
SEQRES  14 A  372  VAL TYR GLN ARG LEU LEU ASP ARG TRP GLY THR SER GLU          
SEQRES  15 A  372  LEU PHE VAL LYS ALA VAL SER LEU GLY SER SER VAL ALA          
SEQRES  16 A  372  THR LEU PRO VAL LYS THR GLU THR GLU PHE THR LYS ALA          
SEQRES  17 A  372  VAL LYS GLU VAL PHE ARG TYR ASP ASP ARG LEU MET VAL          
SEQRES  18 A  372  GLU PRO ARG ILE ARG GLY ARG GLU ILE GLU CYS ALA VAL          
SEQRES  19 A  372  LEU GLY ASN GLY ALA PRO LYS ALA SER LEU PRO GLY GLU          
SEQRES  20 A  372  ILE ILE PRO HIS HIS ASP TYR TYR SER TYR ASP ALA LYS          
SEQRES  21 A  372  TYR LEU ASP PRO ASN GLY ALA THR THR THR THR SER VAL          
SEQRES  22 A  372  ASP LEU SER GLU SER VAL THR LYS GLN ILE GLN GLN ILE          
SEQRES  23 A  372  ALA ILE ASP ALA PHE LYS MET VAL HIS CYS SER GLY MET          
SEQRES  24 A  372  ALA ARG VAL ASP PHE PHE VAL THR PRO ASN ASN LYS VAL          
SEQRES  25 A  372  LEU VAL ASN GLU ILE ASN THR ILE PRO GLY PHE THR ASN          
SEQRES  26 A  372  ILE SER MET TYR PRO LYS MET TRP GLU ALA SER GLY LEU          
SEQRES  27 A  372  PRO CYS PRO ASN LEU LEU ASP GLN LEU ILE GLU LEU ALA          
SEQRES  28 A  372  ILE ASP ARG HIS GLN GLU GLN GLN LYS LEU ILE ARG CYS          
SEQRES  29 A  372  TYR GLU VAL LYS ALA ARG SER LEU                              
SEQRES   1 B  372  MET ALA GLU LYS LEU HIS ILE SER VAL LEU CYS GLY GLY          
SEQRES   2 B  372  GLN SER THR GLU HIS GLU ILE SER ILE GLN SER ALA LYS          
SEQRES   3 B  372  ASN ILE VAL ASN THR LEU ASP ALA ALA LYS TYR LEU ILE          
SEQRES   4 B  372  SER VAL ILE PHE ILE ASP HIS VAL GLY ARG TRP TYR LEU          
SEQRES   5 B  372  ILE ASP GLN PRO GLU MET PHE LEU ALA HIS SER PRO ASP          
SEQRES   6 B  372  HIS LEU VAL LYS GLU GLY SER ALA ARG PRO ILE THR ILE          
SEQRES   7 B  372  ALA PHE GLY ASP ALA ALA LYS PRO TRP GLN SER LEU ASN          
SEQRES   8 B  372  GLY ASP GLY ARG ARG TYR SER ALA ASP CYS VAL PHE PRO          
SEQRES   9 B  372  MET VAL HIS GLY THR GLN GLY GLU ASP GLY ALA LEU GLN          
SEQRES  10 B  372  GLY LEU LEU GLU LEU LEU ASN LEU PRO TYR VAL GLY ALA          
SEQRES  11 B  372  ASN VAL GLN SER SER ALA VAL CYS MET GLU LYS ASP LEU          
SEQRES  12 B  372  THR LYS THR VAL LEU ARG ALA GLY GLY ILE PRO VAL VAL          
SEQRES  13 B  372  ASP TRP HIS THR LEU SER PRO ARG ASP ALA THR GLU GLY          
SEQRES  14 B  372  VAL TYR GLN ARG LEU LEU ASP ARG TRP GLY THR SER GLU          
SEQRES  15 B  372  LEU PHE VAL LYS ALA VAL SER LEU GLY SER SER VAL ALA          
SEQRES  16 B  372  THR LEU PRO VAL LYS THR GLU THR GLU PHE THR LYS ALA          
SEQRES  17 B  372  VAL LYS GLU VAL PHE ARG TYR ASP ASP ARG LEU MET VAL          
SEQRES  18 B  372  GLU PRO ARG ILE ARG GLY ARG GLU ILE GLU CYS ALA VAL          
SEQRES  19 B  372  LEU GLY ASN GLY ALA PRO LYS ALA SER LEU PRO GLY GLU          
SEQRES  20 B  372  ILE ILE PRO HIS HIS ASP TYR TYR SER TYR ASP ALA LYS          
SEQRES  21 B  372  TYR LEU ASP PRO ASN GLY ALA THR THR THR THR SER VAL          
SEQRES  22 B  372  ASP LEU SER GLU SER VAL THR LYS GLN ILE GLN GLN ILE          
SEQRES  23 B  372  ALA ILE ASP ALA PHE LYS MET VAL HIS CYS SER GLY MET          
SEQRES  24 B  372  ALA ARG VAL ASP PHE PHE VAL THR PRO ASN ASN LYS VAL          
SEQRES  25 B  372  LEU VAL ASN GLU ILE ASN THR ILE PRO GLY PHE THR ASN          
SEQRES  26 B  372  ILE SER MET TYR PRO LYS MET TRP GLU ALA SER GLY LEU          
SEQRES  27 B  372  PRO CYS PRO ASN LEU LEU ASP GLN LEU ILE GLU LEU ALA          
SEQRES  28 B  372  ILE ASP ARG HIS GLN GLU GLN GLN LYS LEU ILE ARG CYS          
SEQRES  29 B  372  TYR GLU VAL LYS ALA ARG SER LEU                              
FORMUL   3  HOH   *490(H2 O)                                                    
HELIX    1   1 GLU A   17  LEU A   32  1                                  16    
HELIX    2   2 GLN A   55  HIS A   62  1                                   8    
HELIX    3   3 SER A   63  GLY A   71  1                                   9    
HELIX    4   4 GLY A  114  LEU A  123  1                                  10    
HELIX    5   5 ASN A  131  GLU A  140  1                                  10    
HELIX    6   6 GLU A  140  GLY A  151  1                                  12    
HELIX    7   7 GLY A  169  TRP A  178  1                                  10    
HELIX    8   8 SER A  192  VAL A  194  5                                   3    
HELIX    9   9 THR A  201  PHE A  213  1                                  13    
HELIX   10  10 SER A  276  VAL A  294  1                                  19    
HELIX   11  11 SER A  327  SER A  336  1                                  10    
HELIX   12  12 PRO A  339  SER A  371  1                                  33    
HELIX   13  13 GLU B   17  LEU B   32  1                                  16    
HELIX   14  14 GLN B   55  HIS B   62  1                                   8    
HELIX   15  15 SER B   63  GLY B   71  1                                   9    
HELIX   16  16 GLY B  114  LEU B  123  1                                  10    
HELIX   17  17 ASN B  131  GLU B  140  1                                  10    
HELIX   18  18 GLU B  140  GLY B  151  1                                  12    
HELIX   19  19 GLY B  169  GLY B  179  1                                  11    
HELIX   20  20 SER B  192  VAL B  194  5                                   3    
HELIX   21  21 THR B  201  PHE B  213  1                                  13    
HELIX   22  22 GLU B  277  VAL B  294  1                                  18    
HELIX   23  23 SER B  327  SER B  336  1                                  10    
HELIX   24  24 PRO B  339  LYS B  368  1                                  30    
SHEET    1   A 7 ARG A  96  TYR A  97  0                                        
SHEET    2   A 7 TRP A  87  SER A  89 -1  N  TRP A  87   O  TYR A  97           
SHEET    3   A 7 ARG A  74  ILE A  78 -1  N  THR A  77   O  GLN A  88           
SHEET    4   A 7 TRP A  50  ILE A  53 -1  N  LEU A  52   O  ARG A  74           
SHEET    5   A 7 TYR A  37  ILE A  44 -1  N  VAL A  41   O  ILE A  53           
SHEET    6   A 7 LEU A   5  GLY A  12  1  N  VAL A   9   O  ILE A  42           
SHEET    7   A 7 CYS A 101  PRO A 104  1  O  PHE A 103   N  SER A   8           
SHEET    1   B 4 HIS A 159  LEU A 161  0                                        
SHEET    2   B 4 LEU A 219  PRO A 223 -1  O  VAL A 221   N  HIS A 159           
SHEET    3   B 4 LEU A 183  ALA A 187 -1  N  PHE A 184   O  GLU A 222           
SHEET    4   B 4 THR A 196  VAL A 199 -1  O  LEU A 197   N  VAL A 185           
SHEET    1   C 4 LYS A 241  ALA A 242  0                                        
SHEET    2   C 4 ARG A 228  GLY A 236 -1  N  LEU A 235   O  LYS A 241           
SHEET    3   C 4 GLY A 246  ILE A 249 -1  O  GLY A 246   N  GLU A 231           
SHEET    4   C 4 THR A 268  THR A 270 -1  O  THR A 268   N  ILE A 249           
SHEET    1   D 4 LYS A 241  ALA A 242  0                                        
SHEET    2   D 4 ARG A 228  GLY A 236 -1  N  LEU A 235   O  LYS A 241           
SHEET    3   D 4 GLY A 298  VAL A 306 -1  O  PHE A 304   N  ILE A 230           
SHEET    4   D 4 VAL A 312  ASN A 318 -1  O  ASN A 315   N  ASP A 303           
SHEET    1   E 7 ARG B  96  TYR B  97  0                                        
SHEET    2   E 7 TRP B  87  SER B  89 -1  N  TRP B  87   O  TYR B  97           
SHEET    3   E 7 ARG B  74  ILE B  78 -1  N  THR B  77   O  GLN B  88           
SHEET    4   E 7 TRP B  50  ILE B  53 -1  N  LEU B  52   O  ARG B  74           
SHEET    5   E 7 TYR B  37  ILE B  44 -1  N  VAL B  41   O  ILE B  53           
SHEET    6   E 7 LEU B   5  GLY B  12  1  N  VAL B   9   O  ILE B  42           
SHEET    7   E 7 CYS B 101  PRO B 104  1  O  PHE B 103   N  SER B   8           
SHEET    1   F 4 HIS B 159  LEU B 161  0                                        
SHEET    2   F 4 LEU B 219  PRO B 223 -1  O  VAL B 221   N  HIS B 159           
SHEET    3   F 4 LEU B 183  ALA B 187 -1  N  LYS B 186   O  MET B 220           
SHEET    4   F 4 THR B 196  VAL B 199 -1  O  VAL B 199   N  LEU B 183           
SHEET    1   G 3 LYS B 241  ALA B 242  0                                        
SHEET    2   G 3 ARG B 228  GLY B 236 -1  N  LEU B 235   O  LYS B 241           
SHEET    3   G 3 GLY B 246  ILE B 248 -1  O  GLY B 246   N  GLU B 231           
SHEET    1   H 4 LYS B 241  ALA B 242  0                                        
SHEET    2   H 4 ARG B 228  GLY B 236 -1  N  LEU B 235   O  LYS B 241           
SHEET    3   H 4 GLY B 298  VAL B 306 -1  O  PHE B 304   N  ILE B 230           
SHEET    4   H 4 VAL B 312  ASN B 318 -1  O  ASN B 315   N  ASP B 303           
CRYST1   68.238   97.442  106.563  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      0.014655  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010263  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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