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Database: PDB
Entry: 4ZUY
LinkDB: 4ZUY
Original site: 4ZUY 
HEADER    PROTEIN BINDING                         18-MAY-15   4ZUY              
TITLE     STRUCTURE OF TSI6 FROM PSEUDOMONAS AERUGINOSA                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TSI6;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /     
SOURCE   3 PAO1 / 1C / PRS 101 / LMG 12228);                                    
SOURCE   4 ORGANISM_TAXID: 208964;                                              
SOURCE   5 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;                
SOURCE   6 GENE: PA0092;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET29B                                    
KEYWDS    4-HELIX BUNDLE, BACTERIAL TYPE VI SECRETION IMMUNITY PROTEIN, TSE6    
KEYWDS   2 IMMUNITY PROTEIN, PROTEIN BINDING                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.WHITNEY,S.SAWAI,H.ROBINSON,J.D.MOUGOUS                            
REVDAT   4   11-DEC-19 4ZUY    1       REMARK                                   
REVDAT   3   24-APR-19 4ZUY    1       REMARK                                   
REVDAT   2   20-SEP-17 4ZUY    1       REMARK                                   
REVDAT   1   11-NOV-15 4ZUY    0                                                
JRNL        AUTH   J.C.WHITNEY,D.QUENTIN,S.SAWAI,M.LEROUX,B.N.HARDING,          
JRNL        AUTH 2 H.E.LEDVINA,B.Q.TRAN,H.ROBINSON,Y.A.GOO,D.R.GOODLETT,        
JRNL        AUTH 3 S.RAUNSER,J.D.MOUGOUS                                        
JRNL        TITL   AN INTERBACTERIAL NAD(P)(+) GLYCOHYDROLASE TOXIN REQUIRES    
JRNL        TITL 2 ELONGATION FACTOR TU FOR DELIVERY TO TARGET CELLS.           
JRNL        REF    CELL                          V. 163   607 2015              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   26456113                                                     
JRNL        DOI    10.1016/J.CELL.2015.09.027                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18765                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1869                            
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 47.9800 -  4.5889    1.00     1410   158  0.1811 0.2115        
REMARK   3     2  4.5889 -  3.6427    0.98     1327   148  0.1631 0.1925        
REMARK   3     3  3.6427 -  3.1824    0.99     1317   144  0.2005 0.2443        
REMARK   3     4  3.1824 -  2.8914    1.00     1329   150  0.2212 0.2899        
REMARK   3     5  2.8914 -  2.6842    1.00     1317   142  0.2083 0.2762        
REMARK   3     6  2.6842 -  2.5260    1.00     1309   144  0.1992 0.3004        
REMARK   3     7  2.5260 -  2.3995    1.00     1288   145  0.1976 0.2358        
REMARK   3     8  2.3995 -  2.2950    0.99     1290   145  0.2001 0.2590        
REMARK   3     9  2.2950 -  2.2067    0.99     1297   138  0.2006 0.2314        
REMARK   3    10  2.2067 -  2.1305    0.98     1287   150  0.2026 0.2424        
REMARK   3    11  2.1305 -  2.0639    0.98     1263   136  0.2060 0.2627        
REMARK   3    12  2.0639 -  2.0049    0.98     1295   141  0.2186 0.2659        
REMARK   3    13  2.0049 -  1.9521    0.91     1167   128  0.2477 0.2662        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.007           1472                                  
REMARK   3   ANGLE     :  0.933           1991                                  
REMARK   3   CHIRALITY :  0.038            233                                  
REMARK   3   PLANARITY :  0.004            253                                  
REMARK   3   DIHEDRAL  : 14.241            565                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 20 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7942 -13.4023  13.6926              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4574 T22:   0.4285                                     
REMARK   3      T33:   0.3159 T12:  -0.0088                                     
REMARK   3      T13:   0.1042 T23:  -0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7651 L22:   4.9425                                     
REMARK   3      L33:   4.5316 L12:   0.0158                                     
REMARK   3      L13:   0.5235 L23:  -1.9805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1949 S12:  -0.6533 S13:   0.1426                       
REMARK   3      S21:   0.6243 S22:  -0.0920 S23:   0.5776                       
REMARK   3      S31:  -0.2869 S32:  -0.5104 S33:  -0.0839                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 42 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6650 -16.5745  11.6180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3915 T22:   0.4931                                     
REMARK   3      T33:   0.5002 T12:   0.0585                                     
REMARK   3      T13:  -0.0421 T23:   0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8992 L22:   3.1032                                     
REMARK   3      L33:   4.2259 L12:   1.3044                                     
REMARK   3      L13:  -1.0417 L23:  -1.0655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5065 S12:  -0.5241 S13:   0.0103                       
REMARK   3      S21:  -0.1002 S22:  -0.0825 S23:  -0.8465                       
REMARK   3      S31:   0.3099 S32:   0.0147 S33:   0.5674                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4930  -3.4823   2.0746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9637 T22:   0.6213                                     
REMARK   3      T33:   0.5493 T12:  -0.2122                                     
REMARK   3      T13:  -0.0110 T23:   0.1158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8904 L22:   2.8402                                     
REMARK   3      L33:   5.1035 L12:  -3.3964                                     
REMARK   3      L13:   3.1120 L23:  -0.5472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0718 S12:  -1.0882 S13:   0.6009                       
REMARK   3      S21:  -0.6085 S22:  -0.1369 S23:  -1.3209                       
REMARK   3      S31:  -0.6290 S32:  -0.5102 S33:  -0.1773                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3662 -15.9877   0.0144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2989 T22:   0.5798                                     
REMARK   3      T33:   0.3433 T12:  -0.0022                                     
REMARK   3      T13:  -0.0066 T23:  -0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5612 L22:   2.0217                                     
REMARK   3      L33:   3.9692 L12:  -1.4488                                     
REMARK   3      L13:   1.7001 L23:   4.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2172 S12:   0.8941 S13:  -1.1147                       
REMARK   3      S21:   0.3409 S22:  -0.0976 S23:  -1.3352                       
REMARK   3      S31:   0.1493 S32:   1.0870 S33:   0.1287                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 88 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3927 -18.2889   4.1370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2796 T22:   0.3185                                     
REMARK   3      T33:   0.3481 T12:   0.0367                                     
REMARK   3      T13:   0.0656 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3531 L22:   4.1592                                     
REMARK   3      L33:   6.5359 L12:   1.1084                                     
REMARK   3      L13:   0.9445 L23:   0.9194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2398 S12:  -0.2146 S13:  -0.2914                       
REMARK   3      S21:   0.0512 S22:   0.3199 S23:   0.3383                       
REMARK   3      S31:   0.2668 S32:  -0.4292 S33:  -0.0090                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1499   7.0034   0.0664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5311 T22:   0.3803                                     
REMARK   3      T33:   0.6333 T12:  -0.0912                                     
REMARK   3      T13:   0.0378 T23:  -0.1098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7331 L22:   7.4103                                     
REMARK   3      L33:   0.5735 L12:  -5.9794                                     
REMARK   3      L13:  -0.6638 L23:   0.8137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0631 S12:   0.6602 S13:  -0.1614                       
REMARK   3      S21:  -0.1419 S22:  -0.5169 S23:   0.9000                       
REMARK   3      S31:   0.5891 S32:  -0.7312 S33:  -0.5145                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 42 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7197 -20.0403 -15.9940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3779 T22:   0.3896                                     
REMARK   3      T33:   0.3659 T12:  -0.0292                                     
REMARK   3      T13:  -0.0013 T23:  -0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8942 L22:   2.6344                                     
REMARK   3      L33:   0.7677 L12:   0.4103                                     
REMARK   3      L13:  -0.3204 L23:  -0.2319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1267 S12:   0.3062 S13:   0.1170                       
REMARK   3      S21:  -0.2564 S22:   0.0601 S23:   0.1630                       
REMARK   3      S31:  -0.0968 S32:  -0.0906 S33:   0.0928                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1167 -32.6585  -4.8256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3885 T22:   0.4459                                     
REMARK   3      T33:   0.7218 T12:  -0.0593                                     
REMARK   3      T13:  -0.0376 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1343 L22:   0.6411                                     
REMARK   3      L33:   2.0014 L12:   0.3113                                     
REMARK   3      L13:   1.2013 L23:  -0.6681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2309 S12:  -0.9246 S13:   0.2743                       
REMARK   3      S21:   0.8658 S22:   0.1612 S23:   0.3366                       
REMARK   3      S31:  -0.6564 S32:  -0.0017 S33:   0.1532                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 51 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1460 -16.4939  -7.5662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2850 T22:   0.2696                                     
REMARK   3      T33:   0.2817 T12:  -0.0267                                     
REMARK   3      T13:   0.0015 T23:  -0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6272 L22:   7.9030                                     
REMARK   3      L33:   4.8356 L12:  -1.6622                                     
REMARK   3      L13:   2.1193 L23:  -0.4214                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0993 S12:   0.1345 S13:  -0.1729                       
REMARK   3      S21:  -0.0223 S22:   0.1114 S23:   0.1500                       
REMARK   3      S31:  -0.2757 S32:   0.1048 S33:  -0.0661                       
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 4ZUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209956.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19003                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 15.00                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68700                            
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: SAD                          
REMARK 200 SOFTWARE USED: SHELXDE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE:HCL PH 8.0, 2.5 M        
REMARK 280  NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.54900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.54900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       27.25550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.47800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       27.25550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.47800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.54900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       27.25550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.47800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.54900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       27.25550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.47800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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     HIS A    97                                                      
REMARK 465     HIS A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     HIS A   100                                                      
REMARK 465     HIS A   101                                                      
REMARK 465     HIS A   102                                                      
REMARK 465     ARG B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     LYS B    90                                                      
REMARK 465     VAL B    91                                                      
REMARK 465     ASP B    92                                                      
REMARK 465     LEU B    93                                                      
REMARK 465     PRO B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     HIS B    97                                                      
REMARK 465     HIS B    98                                                      
REMARK 465     HIS B    99                                                      
REMARK 465     HIS B   100                                                      
REMARK 465     HIS B   101                                                      
REMARK 465     HIS B   102                                                      
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     GLU A  66    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  32    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   341     O    HOH B   345              1.86            
REMARK 500   O    HOH A   327     O    HOH A   346              1.94            
REMARK 500   O    GLU A    96     O    HOH A   301              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  24      105.75    -56.18                                   
REMARK 500    LEU A  95      -10.53     72.88                                   
REMARK 500    ASP B  68       72.91   -150.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 201                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZV4   RELATED DB: PDB                                   
DBREF  4ZUY A    1    94  UNP    Q9I740   Q9I740_PSEAE     1     94             
DBREF  4ZUY B    1    94  UNP    Q9I740   Q9I740_PSEAE     1     94             
SEQADV 4ZUY MSE A   37  UNP  Q9I740    ILE    37 ENGINEERED MUTATION            
SEQADV 4ZUY LEU A   95  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY GLU A   96  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A   97  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A   98  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A   99  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A  100  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A  101  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS A  102  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY MSE B   37  UNP  Q9I740    ILE    37 ENGINEERED MUTATION            
SEQADV 4ZUY LEU B   95  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY GLU B   96  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B   97  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B   98  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B   99  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B  100  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B  101  UNP  Q9I740              EXPRESSION TAG                 
SEQADV 4ZUY HIS B  102  UNP  Q9I740              EXPRESSION TAG                 
SEQRES   1 A  102  MSE THR PRO ILE GLU TYR ILE ASP ARG ALA LEU ALA LEU          
SEQRES   2 A  102  VAL VAL ASP ARG LEU ALA ARG TYR PRO GLY TYR GLU VAL          
SEQRES   3 A  102  LEU LEU SER ALA GLU LYS GLN LEU GLN TYR MSE ARG SER          
SEQRES   4 A  102  VAL LEU LEU ASP ARG SER LEU ASP ARG SER ALA LEU HIS          
SEQRES   5 A  102  ARG LEU THR LEU GLY SER ILE ALA VAL LYS GLU PHE ASP          
SEQRES   6 A  102  GLU THR ASP PRO GLU LEU SER ARG ALA LEU LYS ASP ALA          
SEQRES   7 A  102  TYR TYR VAL GLY ILE ARG THR GLY ARG GLY LEU LYS VAL          
SEQRES   8 A  102  ASP LEU PRO LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  102  MSE THR PRO ILE GLU TYR ILE ASP ARG ALA LEU ALA LEU          
SEQRES   2 B  102  VAL VAL ASP ARG LEU ALA ARG TYR PRO GLY TYR GLU VAL          
SEQRES   3 B  102  LEU LEU SER ALA GLU LYS GLN LEU GLN TYR MSE ARG SER          
SEQRES   4 B  102  VAL LEU LEU ASP ARG SER LEU ASP ARG SER ALA LEU HIS          
SEQRES   5 B  102  ARG LEU THR LEU GLY SER ILE ALA VAL LYS GLU PHE ASP          
SEQRES   6 B  102  GLU THR ASP PRO GLU LEU SER ARG ALA LEU LYS ASP ALA          
SEQRES   7 B  102  TYR TYR VAL GLY ILE ARG THR GLY ARG GLY LEU LYS VAL          
SEQRES   8 B  102  ASP LEU PRO LEU GLU HIS HIS HIS HIS HIS HIS                  
MODRES 4ZUY MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 4ZUY MSE B    1  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  37       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  37       8                                                       
HET     CL  A 201       1                                                       
HET     CL  A 202       1                                                       
HET     CL  A 203       1                                                       
HET     CL  B 201       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3   CL    4(CL 1-)                                                     
FORMUL   7  HOH   *98(H2 O)                                                     
HELIX    1 AA1 THR A    2  TYR A   21  1                                  20    
HELIX    2 AA2 TYR A   24  ASP A   43  1                                  20    
HELIX    3 AA3 ARG A   48  LEU A   54  5                                   7    
HELIX    4 AA4 THR A   55  ASP A   65  1                                  11    
HELIX    5 AA5 ASP A   68  ARG A   84  1                                  17    
HELIX    6 AA6 THR A   85  LEU A   89  5                                   5    
HELIX    7 AA7 THR B    2  TYR B   21  1                                  20    
HELIX    8 AA8 TYR B   24  ASP B   43  1                                  20    
HELIX    9 AA9 ALA B   50  LEU B   54  5                                   5    
HELIX   10 AB1 THR B   55  ASP B   65  1                                  11    
HELIX   11 AB2 ASP B   68  ARG B   84  1                                  17    
LINK         C   MSE A   1                 N   THR A   2     1555   1555  1.32  
LINK         C   TYR A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   ARG A  38     1555   1555  1.33  
LINK         C   MSE B   1                 N   THR B   2     1555   1555  1.33  
LINK         C   TYR B  36                 N   MSE B  37     1555   1555  1.33  
LINK         C   MSE B  37                 N   ARG B  38     1555   1555  1.33  
SITE     1 AC1  2 LYS A  76  THR B  85                                          
SITE     1 AC2  2 THR A  85  LYS B  76                                          
SITE     1 AC3  3 ARG A  84  LYS A  90  ASP A  92                               
SITE     1 AC4  2 ARG B  73  ASP B  77                                          
CRYST1   54.511  100.956   93.098  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018345  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010741        0.00000                         
HETATM    1  N   MSE A   1     -20.474  -3.156   5.919  1.00 56.03           N  
ANISOU    1  N   MSE A   1     7053   6227   8008   2050    979   -838       N  
HETATM    2  CA  MSE A   1     -19.356  -3.879   6.505  1.00 58.16           C  
ANISOU    2  CA  MSE A   1     7501   6550   8048   1777    989   -891       C  
HETATM    3  C   MSE A   1     -18.066  -3.568   5.773  1.00 54.86           C  
ANISOU    3  C   MSE A   1     7386   5935   7522   1647    807   -920       C  
HETATM    4  O   MSE A   1     -18.047  -3.422   4.548  1.00 53.94           O  
ANISOU    4  O   MSE A   1     7288   5706   7499   1673    610   -835       O  
HETATM    5  CB  MSE A   1     -19.606  -5.382   6.475  1.00 56.53           C  
ANISOU    5  CB  MSE A   1     7053   6562   7864   1574    909   -748       C  
HETATM    6  CG  MSE A   1     -20.674  -5.852   7.429  1.00 65.50           C  
ANISOU    6  CG  MSE A   1     7893   7929   9066   1622   1125   -700       C  
HETATM    7 SE   MSE A   1     -19.944  -6.307   9.164  0.77 78.88          SE  
ANISOU    7 SE   MSE A   1     9771   9748  10453   1461   1387   -819      SE  
HETATM    8  CE  MSE A   1     -18.916  -7.899   8.695  1.00 65.02           C  
ANISOU    8  CE  MSE A   1     8067   8042   8595   1098   1118   -698       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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