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Database: PDB
Entry: 4UQZ
LinkDB: 4UQZ
Original site: 4UQZ 
HEADER    PROTEIN TRANSPORT                       25-JUN-14   4UQZ              
TITLE     COEVOLUTION OF THE ATPASE CLPV, THE TSSB-TSSC SHEATH AND              
TITLE    2 THE ACCESSORY HSIE PROTEIN DISTINGUISHES TWO TYPE VI                 
TITLE    3 SECRETION CLASSES                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HSIE1;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-281;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HSIB1;                                                     
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: PROTEIN DEGRADED DURING PURIFICATION                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;                    
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PACYC;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;                    
SOURCE  10 ORGANISM_TAXID: 208964;                                              
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: B384;                                      
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: PACYC                                      
KEYWDS    PROTEIN TRANSPORT, SECRETION, SHEATH, DISASSEMBLY, REGULATION,        
KEYWDS   2 BACTERIAL                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.FORSTER,S.PLANAMENTE,E.MANOLI,N.S.LOSSI,P.S.FREEMONT,A.FILLOUX      
REVDAT   2   03-DEC-14 4UQZ    1       JRNL                                     
REVDAT   1   22-OCT-14 4UQZ    0                                                
JRNL        AUTH   A.FORSTER,S.PLANAMENTE,E.MANOLI,N.S.LOSSI,P.S.FREEMONT,      
JRNL        AUTH 2 A.FILLOUX                                                    
JRNL        TITL   COEVOLUTION OF THE ATPASE CLPV, THE SHEATH PROTEINS TSSB     
JRNL        TITL 2 AND TSSC AND THE ACCESSORY PROTEIN TAGJ/HSIE1 DISTINGUISHES  
JRNL        TITL 3 TYPE VI SECRETION CLASSES.                                   
JRNL        REF    RNA                           V.  20  1955 2014              
JRNL        REFN                   ISSN 1355-8382                               
JRNL        PMID   25305017                                                     
JRNL        DOI    10.1074/JBC.M114.600510                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.599                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.209                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.03                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.59                          
REMARK   3   NUMBER OF REFLECTIONS             : 41994                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1893                          
REMARK   3   R VALUE            (WORKING SET) : 0.1876                          
REMARK   3   FREE R VALUE                     : 0.2206                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4003                            
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 41.2224 -  4.9112    0.99     2708   190  0.1546 0.1943        
REMARK   3     2  4.9112 -  3.8991    1.00     2733   165  0.1337 0.1519        
REMARK   3     3  3.8991 -  3.4065    1.00     2776   130  0.1492 0.1846        
REMARK   3     4  3.4065 -  3.0951    1.00     2762   134  0.1692 0.2019        
REMARK   3     5  3.0951 -  2.8734    0.96     2681   132  0.1781 0.2070        
REMARK   3     6  2.8734 -  2.7040    0.98     2719   119  0.1898 0.2378        
REMARK   3     7  2.7040 -  2.5686    0.98     2735   130  0.1813 0.2166        
REMARK   3     8  2.5686 -  2.4568    0.99     2727   148  0.1774 0.1938        
REMARK   3     9  2.4568 -  2.3622    0.99     2734   127  0.1764 0.1832        
REMARK   3    10  2.3622 -  2.2807    0.95     2686   109  0.1918 0.2254        
REMARK   3    11  2.2807 -  2.2094    0.94     2598   140  0.2744 0.3004        
REMARK   3    12  2.2094 -  2.1463    0.93     2576   114  0.1940 0.2993        
REMARK   3    13  2.1463 -  2.0898    0.99     2709   168  0.1759 0.2219        
REMARK   3    14  2.0898 -  2.0388    0.98     2692   166  0.1741 0.2005        
REMARK   3    15  2.0388 -  1.9924    0.98     2721   130  0.1845 0.2539        
REMARK   3    16  1.9924 -  1.9500    0.95     2594   173  0.2104 0.2138        
REMARK   3    17  1.9500 -  1.9110    0.93     2543   147  0.3479 0.4007        
REMARK   3    18  1.9110 -  1.8750    0.87     2402   137  0.3065 0.2991        
REMARK   3    19  1.8750 -  1.8415    0.92     2586   119  0.2386 0.2207        
REMARK   3    20  1.8415 -  1.8103    0.96     2563   175  0.2231 0.2776        
REMARK   3    21  1.8103 -  1.7811    0.97     2743   111  0.2031 0.3073        
REMARK   3    22  1.7811 -  1.7537    0.95     2676   139  0.2113 0.2559        
REMARK   3    23  1.7537 -  1.7279    0.95     2624   145  0.2157 0.2697        
REMARK   3    24  1.7279 -  1.7035    0.91     2514   136  0.2133 0.2091        
REMARK   3    25  1.7035 -  1.6805    0.91     2506   141  0.2243 0.2480        
REMARK   3    26  1.6805 -  1.6587    0.88     2469   106  0.2277 0.3076        
REMARK   3    27  1.6587 -  1.6379    0.88     2413   125  0.2250 0.2917        
REMARK   3    28  1.6379 -  1.6182    0.86     2415   136  0.2547 0.3093        
REMARK   3    29  1.6182 -  1.5994    0.82     2278   111  0.2632 0.2911        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.18             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.04            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.52                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.012           2238                                  
REMARK   3   ANGLE     :  1.414           3051                                  
REMARK   3   CHIRALITY :  0.066            348                                  
REMARK   3   PLANARITY :  0.007            405                                  
REMARK   3   DIHEDRAL  : 13.614            819                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 88 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3134   9.0216 -48.0314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2647 T22:   0.2155                                     
REMARK   3      T33:   0.1464 T12:  -0.0469                                     
REMARK   3      T13:  -0.0582 T23:   0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0262 L22:   2.6672                                     
REMARK   3      L33:   3.8246 L12:  -0.6930                                     
REMARK   3      L13:  -0.5879 L23:   0.2874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0527 S12:   0.3187 S13:   0.2370                       
REMARK   3      S21:  -0.4604 S22:  -0.0046 S23:  -0.0762                       
REMARK   3      S31:  -0.4601 S32:  -0.0064 S33:   0.0423                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 156 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0321   0.2565 -20.9051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1347 T22:   0.1359                                     
REMARK   3      T33:   0.1750 T12:  -0.0317                                     
REMARK   3      T13:  -0.0238 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2784 L22:   0.8360                                     
REMARK   3      L33:   5.7424 L12:  -0.6490                                     
REMARK   3      L13:  -2.6217 L23:   0.3485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:   0.1803 S13:  -0.1349                       
REMARK   3      S21:   0.0472 S22:  -0.0133 S23:   0.0875                       
REMARK   3      S31:   0.0324 S32:  -0.3030 S33:   0.0559                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2931   9.6604 -21.8002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0852 T22:   0.1017                                     
REMARK   3      T33:   0.1287 T12:  -0.0117                                     
REMARK   3      T13:  -0.0252 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6086 L22:   2.0120                                     
REMARK   3      L33:   2.4018 L12:   0.2369                                     
REMARK   3      L13:  -0.0599 L23:   0.0050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0144 S12:  -0.0433 S13:  -0.0127                       
REMARK   3      S21:   0.1825 S22:   0.0090 S23:  -0.1079                       
REMARK   3      S31:  -0.0556 S32:   0.1593 S33:   0.0044                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 12 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0366  13.9859  -8.1437              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3981 T22:   0.2628                                     
REMARK   3      T33:   0.2531 T12:   0.0916                                     
REMARK   3      T13:   0.0273 T23:  -0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1750 L22:   7.5149                                     
REMARK   3      L33:   0.6676 L12:  -0.6809                                     
REMARK   3      L13:  -0.6400 L23:  -2.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2202 S12:  -0.4140 S13:   0.7533                       
REMARK   3      S21:   1.1454 S22:   0.4094 S23:   0.2968                       
REMARK   3      S31:  -1.1294 S32:  -0.7375 S33:  -0.6170                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 13 THROUGH 22 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4952  22.8942 -21.9834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2807 T22:   0.2001                                     
REMARK   3      T33:   0.2463 T12:   0.0203                                     
REMARK   3      T13:  -0.0259 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0025 L22:   6.9395                                     
REMARK   3      L33:   8.1658 L12:  -0.3307                                     
REMARK   3      L13:  -4.9042 L23:   0.3075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2677 S12:  -0.0837 S13:  -0.1347                       
REMARK   3      S21:   0.6420 S22:   0.0853 S23:   0.2802                       
REMARK   3      S31:   0.0197 S32:   0.0902 S33:   0.2088                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 31 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7340  13.2928 -41.2725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3326 T22:   0.2883                                     
REMARK   3      T33:   0.2557 T12:  -0.1245                                     
REMARK   3      T13:   0.0401 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0303 L22:   0.9536                                     
REMARK   3      L33:   6.6375 L12:  -0.5010                                     
REMARK   3      L13:  -2.2807 L23:   2.4020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1284 S12:   0.4414 S13:   0.0491                       
REMARK   3      S21:  -0.3537 S22:   0.5678 S23:  -0.4682                       
REMARK   3      S31:  -0.5710 S32:   0.5947 S33:  -0.4193                       
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 4UQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61094.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43478                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.70                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.5                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.0                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.40                              
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) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.44                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
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: PDB ENTRY 1ZBP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS(PH 8.0), 24% PEG6000, 0.2    
REMARK 280  M CACL2                                                             
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       26.05600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.01250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.66150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.01250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.05600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.66150            
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: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 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    29                                                      
REMARK 465     ASP A   288                                                      
REMARK 465     ALA A   289                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     LEU B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     PHE B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     MET B    40                                                      
REMARK 465     GLY B    41                                                      
REMARK 465     VAL B    42                                                      
REMARK 465     MET B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     ALA B    51                                                      
REMARK 465     GLU B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     GLN B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     ARG B    60                                                      
REMARK 465     LYS B    61                                                      
REMARK 465     PHE B    62                                                      
REMARK 465     LEU B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     ILE B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     ASP B    68                                                      
REMARK 465     ASN B    69                                                      
REMARK 465     PHE B    70                                                      
REMARK 465     ASP B    71                                                      
REMARK 465     ALA B    72                                                      
REMARK 465     ARG B    73                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     MET B    77                                                      
REMARK 465     LYS B    78                                                      
REMARK 465     PRO B    79                                                      
REMARK 465     ARG B    80                                                      
REMARK 465     VAL B    81                                                      
REMARK 465     ALA B    82                                                      
REMARK 465     PHE B    83                                                      
REMARK 465     ASN B    84                                                      
REMARK 465     VAL B    85                                                      
REMARK 465     PRO B    86                                                      
REMARK 465     ASN B    87                                                      
REMARK 465     VAL B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     THR B    90                                                      
REMARK 465     GLY B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     GLY B    93                                                      
REMARK 465     ASN B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     SER B    96                                                      
REMARK 465     LEU B    97                                                      
REMARK 465     ASP B    98                                                      
REMARK 465     ILE B    99                                                      
REMARK 465     THR B   100                                                      
REMARK 465     PHE B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     SER B   103                                                      
REMARK 465     MET B   104                                                      
REMARK 465     ASP B   105                                                      
REMARK 465     ASP B   106                                                      
REMARK 465     PHE B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     PRO B   109                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     ALA B   111                                                      
REMARK 465     VAL B   112                                                      
REMARK 465     ALA B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     LYS B   115                                                      
REMARK 465     VAL B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     LEU B   119                                                      
REMARK 465     ASN B   120                                                      
REMARK 465     LYS B   121                                                      
REMARK 465     LEU B   122                                                      
REMARK 465     LEU B   123                                                      
REMARK 465     GLU B   124                                                      
REMARK 465     ALA B   125                                                      
REMARK 465     ARG B   126                                                      
REMARK 465     THR B   127                                                      
REMARK 465     GLN B   128                                                      
REMARK 465     LEU B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     LEU B   132                                                      
REMARK 465     LEU B   133                                                      
REMARK 465     THR B   134                                                      
REMARK 465     TYR B   135                                                      
REMARK 465     MET B   136                                                      
REMARK 465     ASP B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 465     LYS B   139                                                      
REMARK 465     THR B   140                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     ALA B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     GLU B   144                                                      
REMARK 465     MET B   145                                                      
REMARK 465     ILE B   146                                                      
REMARK 465     MET B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     ILE B   150                                                      
REMARK 465     LYS B   151                                                      
REMARK 465     ASP B   152                                                      
REMARK 465     PRO B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     LEU B   155                                                      
REMARK 465     LEU B   156                                                      
REMARK 465     GLN B   157                                                      
REMARK 465     ALA B   158                                                      
REMARK 465     LEU B   159                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     ALA B   162                                                      
REMARK 465     PRO B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     PRO B   165                                                      
REMARK 465     LYS B   166                                                      
REMARK 465     ASP B   167                                                      
REMARK 465     ASP B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     GLN B   171                                                      
REMARK 465     ALA B   172                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN B   8    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  31    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    GLY A   272     O    HOH A  2268              2.09            
REMARK 500   O    HOH A  2002     O    HOH B  2013              2.15            
REMARK 500   O    HOH A  2022     O    HOH A  2033              2.13            
REMARK 500   O    HOH A  2028     O    HOH A  2059              2.17            
REMARK 500   O    HOH A  2080     O    HOH A  2134              2.17            
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    ARG A 280      -55.61   -123.17                                   
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 A2020        DISTANCE =  6.43 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UQN   RELATED DB: PDB                                   
REMARK 900  TFL1 FORMS A COMPLEX WITH 14-3-3 AND INHIBITS                       
REMARK 900  FLOWERING BY RECRUITING FD AWAY FROM FT CONTAINING                  
REMARK 900  ACTIVATOR COMPLEX                                                   
REMARK 900 RELATED ID: 4UQW   RELATED DB: PDB                                   
REMARK 900  COEVOLUTION OF THE ATPASE CLPV, THE TSSB-TSSC SHEATH                
REMARK 900  AND THE ACCESSORY HSIE PROTEIN DISTINGUISHES TWO TYPE               
REMARK 900  VI SECRETION CLASSES                                                
REMARK 900 RELATED ID: 4UQX   RELATED DB: PDB                                   
REMARK 900  COEVOLUTION OF THE ATPASE CLPV, THE TSSB-TSSC SHEATH                
REMARK 900  AND THE ACCESSORY HSIE PROTEIN DISTINGUISHES TWO TYPE               
REMARK 900  VI SECRETION CLASSES                                                
REMARK 900 RELATED ID: 4UQY   RELATED DB: PDB                                   
REMARK 900  COEVOLUTION OF THE ATPASE CLPV, THE TSSB-TSSC SHEATH                
REMARK 900  AND THE ACCESSORY HSIE PROTEIN DISTINGUISHES TWO TYPE               
REMARK 900  VI SECRETION CLASSES                                                
DBREF  4UQZ A   29   289  UNP    Q9I746   Q9I746_PSEAE    21    281             
DBREF  4UQZ B    1   172  UNP    Q9I749   Q9I749_PSEAE     1    172             
SEQRES   1 A  261  MET ILE ALA GLU GLU LEU LEU ARG ALA GLY ARG LEU ASP          
SEQRES   2 A  261  ASP ALA LEU LYS ALA LEU GLN GLU GLN VAL ARG SER GLN          
SEQRES   3 A  261  PRO SER ASN ALA THR LEU ARG ILE PHE LEU PHE GLN LEU          
SEQRES   4 A  261  LEU ALA VAL MET GLY GLN TRP ALA ARG ALA GLN ASN GLN          
SEQRES   5 A  261  LEU LYS VAL VAL GLY GLU LEU ASP ALA SER ALA LEU PRO          
SEQRES   6 A  261  MET VAL GLN THR TYR SER THR ALA ILE ASP CYS GLU ALA          
SEQRES   7 A  261  LEU ARG ARG GLU VAL PHE ALA GLY ARG LEU THR PRO VAL          
SEQRES   8 A  261  ILE LEU GLY GLN PRO ALA GLU TRP ILE ALA PRO LEU LEU          
SEQRES   9 A  261  GLN ALA LEU SER LEU ASP ALA GLU GLY HIS GLY GLU ALA          
SEQRES  10 A  261  ALA GLN ALA LEU ARG GLU GLN ALA PHE ASP ALA ALA PRO          
SEQRES  11 A  261  ALA VAL PRO GLY ARG ILE GLY GLU ALA PRO PHE ALA TRP          
SEQRES  12 A  261  LEU ALA ASP ALA ASP THR ARG LEU GLY PRO VAL LEU GLU          
SEQRES  13 A  261  VAL ILE VAL ASN GLY ARG TYR ALA TRP LEU PRO MET SER          
SEQRES  14 A  261  ASN LEU ARG SER LEU LYS VAL GLU ALA PRO SER ASP LEU          
SEQRES  15 A  261  ARG ASP LEU VAL TRP LEU PRO ALA GLU LEU THR LEU ALA          
SEQRES  16 A  261  ASN GLY GLY ALA THR VAL ALA LEU LEU PRO ALA ARG TYR          
SEQRES  17 A  261  ALA GLU THR VAL GLU HIS GLY ASP ASP ALA ALA ARG LEU          
SEQRES  18 A  261  GLY ARG LYS THR GLU TRP LEU ASP SER GLY LEU PRO VAL          
SEQRES  19 A  261  GLY GLN ARG LEU PHE VAL THR ASP ALA GLY GLU THR ALA          
SEQRES  20 A  261  LEU PHE ASP LEU ARG GLU LEU ASP PHE GLU PRO THR ASP          
SEQRES  21 A  261  ALA                                                          
SEQRES   1 B  172  MET GLY SER THR THR SER SER GLN LYS PHE ILE ALA ARG          
SEQRES   2 B  172  ASN ARG ALA PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU          
SEQRES   3 B  172  LEU TYR GLY ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL          
SEQRES   4 B  172  MET GLY VAL MET ALA ASP LEU ALA GLY LYS PRO ALA GLU          
SEQRES   5 B  172  PRO GLN ALA ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE          
SEQRES   6 B  172  ASP VAL ASP ASN PHE ASP ALA ARG LEU LYS ALA MET LYS          
SEQRES   7 B  172  PRO ARG VAL ALA PHE ASN VAL PRO ASN VAL LEU THR GLY          
SEQRES   8 B  172  GLU GLY ASN LEU SER LEU ASP ILE THR PHE GLU SER MET          
SEQRES   9 B  172  ASP ASP PHE SER PRO ALA ALA VAL ALA ARG LYS VAL ASP          
SEQRES  10 B  172  SER LEU ASN LYS LEU LEU GLU ALA ARG THR GLN LEU ALA          
SEQRES  11 B  172  ASN LEU LEU THR TYR MET ASP GLY LYS THR GLY ALA GLU          
SEQRES  12 B  172  GLU MET ILE MET LYS ALA ILE LYS ASP PRO ALA LEU LEU          
SEQRES  13 B  172  GLN ALA LEU ALA SER ALA PRO LYS PRO LYS ASP ASP GLU          
SEQRES  14 B  172  PRO GLN ALA                                                  
HET    ACT  A 301       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4  HOH   *314(H2 O)                                                    
HELIX    1   1 ILE A   30  ALA A   37  1                                   8    
HELIX    2   2 ARG A   39  GLN A   54  1                                  16    
HELIX    3   3 ASN A   57  GLY A   72  1                                  16    
HELIX    4   4 GLN A   73  ASP A   88  1                                  16    
HELIX    5   5 ALA A   91  ALA A  113  1                                  23    
HELIX    6   6 TRP A  127  GLU A  140  1                                  14    
HELIX    7   7 HIS A  142  ALA A  157  1                                  16    
HELIX    8   8 LEU A  210  LEU A  213  5                                   4    
HELIX    9   9 GLU A  238  GLY A  243  1                                   6    
HELIX   10  10 ASP A  244  LEU A  249  1                                   6    
HELIX   11  11 PHE A  277  LEU A  279  5                                   3    
SHEET    1  AA 3 VAL A 119  ILE A 120  0                                        
SHEET    2  AA 3 ARG A 190  PRO A 195  1  O  TYR A 191   N  VAL A 119           
SHEET    3  AA 3 VAL A 182  VAL A 187 -1  O  LEU A 183   N  LEU A 194           
SHEET    1  AB 6 ALA A 167  PHE A 169  0                                        
SHEET    2  AB 6 GLY A 162  ILE A 164 -1  O  GLY A 162   N  PHE A 169           
SHEET    3  AB 6 GLU A 281  PHE A 284 -1  O  ASP A 283   N  ARG A 163           
SHEET    4  AB 6 LEU A 199  VAL A 204 -1  O  ARG A 200   N  PHE A 284           
SHEET    5  AB 6 TRP A 215  LEU A 222 -1  O  GLU A 219   N  LYS A 203           
SHEET    6  AB 6 ALA A 227  PRO A 233 -1  O  THR A 228   N  LEU A 220           
SHEET    1  AC 3 LEU A 172  ASP A 174  0                                        
SHEET    2  AC 3 LEU A 266  THR A 269 -1  O  VAL A 268   N  ALA A 173           
SHEET    3  AC 3 GLU A 273  ALA A 275 -1  O  THR A 274   N  PHE A 267           
SHEET    1  AD 3 PRO A 261  GLY A 263  0                                        
SHEET    2  AD 3 LYS A 252  TRP A 255 -1  O  GLU A 254   N  VAL A 262           
SHEET    3  AD 3 ARG B  18  VAL B  19 -1  O  ARG B  18   N  THR A 253           
SITE     1 AC1  5 GLU A  86  HIS A 142  GLY A 143  GLU A 144                    
SITE     2 AC1  5 ALA A 145                                                     
CRYST1   52.112   67.323   94.025  90.00  90.00  90.00 P 21 21 21    4          
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      0.019189  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010635        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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