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Database: PDB
Entry: 4EQM
LinkDB: 4EQM
Original site: 4EQM 
HEADER    TRANSFERASE                             19-APR-12   4EQM              
TITLE     STRUCTURAL ANALYSIS OF STAPHYLOCOCCUS AUREUS SERINE/THREONINE KINASE  
TITLE    2 PKNB                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE;                                            
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 1-291;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 158879;                                              
SOURCE   4 STRAIN: N315;                                                        
SOURCE   5 GENE: SA1063;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, SERINE/THREONINE PROTEIN KINASE, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RAKETTE,T.STEHLE                                                    
REVDAT   2   15-NOV-17 4EQM    1       REMARK                                   
REVDAT   1   27-JUN-12 4EQM    0                                                
JRNL        AUTH   S.RAKETTE,S.DONAT,K.OHLSEN,T.STEHLE                          
JRNL        TITL   STRUCTURAL ANALYSIS OF STAPHYLOCOCCUS AUREUS                 
JRNL        TITL 2 SERINE/THREONINE KINASE PKNB.                                
JRNL        REF    PLOS ONE                      V.   7 39136 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22701750                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0039136                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 38854                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1944                            
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 43.5174 -  7.2203    0.98     2685   142  0.1670 0.1670        
REMARK   3     2  7.2203 -  5.7351    0.99     2639   139  0.2092 0.2432        
REMARK   3     3  5.7351 -  5.0114    0.99     2620   138  0.2158 0.2436        
REMARK   3     4  5.0114 -  4.5537    0.98     2631   138  0.1884 0.2512        
REMARK   3     5  4.5537 -  4.2276    0.99     2650   140  0.1773 0.2287        
REMARK   3     6  4.2276 -  3.9785    0.99     2617   138  0.1931 0.2059        
REMARK   3     7  3.9785 -  3.7794    1.00     2664   140  0.2305 0.2516        
REMARK   3     8  3.7794 -  3.6150    0.98     2618   138  0.2555 0.3087        
REMARK   3     9  3.6150 -  3.4759    1.00     2603   137  0.2932 0.3323        
REMARK   3    10  3.4759 -  3.3560    1.00     2605   137  0.2888 0.3333        
REMARK   3    11  3.3560 -  3.2511    0.99     2649   139  0.2948 0.3515        
REMARK   3    12  3.2511 -  3.1582    1.00     2632   139  0.2965 0.3426        
REMARK   3    13  3.1582 -  3.0750    0.99     2661   140  0.3162 0.3751        
REMARK   3    14  3.0750 -  3.0000    0.99     2636   139  0.3406 0.3954        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.11                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 70.93                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.140           
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) : 12.99810                                             
REMARK   3    B22 (A**2) : 8.35360                                              
REMARK   3    B33 (A**2) : -13.88730                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.28750                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          12822                                  
REMARK   3   ANGLE     :  0.918          17444                                  
REMARK   3   CHIRALITY :  0.078           2043                                  
REMARK   3   PLANARITY :  0.003           2246                                  
REMARK   3   DIHEDRAL  : 16.257           4822                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 18                                          
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:16 )                  
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 7:16 )                  
REMARK   3     ATOM PAIRS NUMBER  : 85                                          
REMARK   3     RMSD               : 0.010                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:16 )                  
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 7:16 )                  
REMARK   3     ATOM PAIRS NUMBER  : 85                                          
REMARK   3     RMSD               : 0.027                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 7:16 )                  
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 7:16 )                  
REMARK   3     ATOM PAIRS NUMBER  : 89                                          
REMARK   3     RMSD               : 0.117                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 7:16 )                  
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 7:16 )                  
REMARK   3     ATOM PAIRS NUMBER  : 89                                          
REMARK   3     RMSD               : 0.342                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 22:29 )                 
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 22:29 )                 
REMARK   3     ATOM PAIRS NUMBER  : 62                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 22:29 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 22:29 )                 
REMARK   3     ATOM PAIRS NUMBER  : 62                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 35:41 )                 
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 35:41 )                 
REMARK   3     ATOM PAIRS NUMBER  : 51                                          
REMARK   3     RMSD               : 0.007                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 35:41 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 35:41 )                 
REMARK   3     ATOM PAIRS NUMBER  : 51                                          
REMARK   3     RMSD               : 0.006                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 22:29 )                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 22:29 )                 
REMARK   3     ATOM PAIRS NUMBER  : 58                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 22:29 )                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 22:29 )                 
REMARK   3     ATOM PAIRS NUMBER  : 58                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 35:41 )                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 35:41 )                 
REMARK   3     ATOM PAIRS NUMBER  : 51                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 35:41 )                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 35:41 )                 
REMARK   3     ATOM PAIRS NUMBER  : 51                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 51:75 )                 
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 51:75 )                 
REMARK   3     ATOM PAIRS NUMBER  : 203                                         
REMARK   3     RMSD               : 0.167                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 51:75 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 51:75 )                 
REMARK   3     ATOM PAIRS NUMBER  : 203                                         
REMARK   3     RMSD               : 0.004                                       
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 83:90 )                 
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 83:90 )                 
REMARK   3     ATOM PAIRS NUMBER  : 76                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 83:90 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 83:90 )                 
REMARK   3     ATOM PAIRS NUMBER  : 76                                          
REMARK   3     RMSD               : 0.006                                       
REMARK   3   NCS GROUP : 9                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 51:75 )                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 51:75 )                 
REMARK   3     ATOM PAIRS NUMBER  : 197                                         
REMARK   3     RMSD               : 0.008                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 51:75 )                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 51:75 )                 
REMARK   3     ATOM PAIRS NUMBER  : 195                                         
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 10                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 83:90 )                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 83:90 )                 
REMARK   3     ATOM PAIRS NUMBER  : 76                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 83:90 )                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 83:90 )                 
REMARK   3     ATOM PAIRS NUMBER  : 76                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 11                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 97:150)                 
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 97:150)                 
REMARK   3     ATOM PAIRS NUMBER  : 427                                         
REMARK   3     RMSD               : 0.009                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 97:150)                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 97:150)                 
REMARK   3     ATOM PAIRS NUMBER  : 427                                         
REMARK   3     RMSD               : 0.031                                       
REMARK   3   NCS GROUP : 12                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 97:150)                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 97:150)                 
REMARK   3     ATOM PAIRS NUMBER  : 423                                         
REMARK   3     RMSD               : 0.073                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 97:150)                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 97:150)                 
REMARK   3     ATOM PAIRS NUMBER  : 423                                         
REMARK   3     RMSD               : 0.075                                       
REMARK   3   NCS GROUP : 13                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 174:250)                
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 174:250)                
REMARK   3     ATOM PAIRS NUMBER  : 585                                         
REMARK   3     RMSD               : 0.022                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 174:250)                
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 174:250)                
REMARK   3     ATOM PAIRS NUMBER  : 585                                         
REMARK   3     RMSD               : 0.021                                       
REMARK   3   NCS GROUP : 14                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 259:272)                
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 259:272)                
REMARK   3     ATOM PAIRS NUMBER  : 111                                         
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 259:272)                
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 259:272)                
REMARK   3     ATOM PAIRS NUMBER  : 111                                         
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 15                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 273:281)                
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 273:281)                
REMARK   3     ATOM PAIRS NUMBER  : 77                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 273:281)                
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 273:281)                
REMARK   3     ATOM PAIRS NUMBER  : 77                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3   NCS GROUP : 16                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 174:250)                
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 174:250)                
REMARK   3     ATOM PAIRS NUMBER  : 571                                         
REMARK   3     RMSD               : 0.160                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 174:250)                
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 174:250)                
REMARK   3     ATOM PAIRS NUMBER  : 571                                         
REMARK   3     RMSD               : 0.011                                       
REMARK   3   NCS GROUP : 17                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 259:272)                
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 259:272)                
REMARK   3     ATOM PAIRS NUMBER  : 111                                         
REMARK   3     RMSD               : 0.514                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 259:272)                
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 259:272)                
REMARK   3     ATOM PAIRS NUMBER  : 111                                         
REMARK   3     RMSD               : 0.133                                       
REMARK   3   NCS GROUP : 18                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 273:281)                
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 273:281)                
REMARK   3     ATOM PAIRS NUMBER  : 71                                          
REMARK   3     RMSD               : 0.005                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 273:281)                
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 273:281)                
REMARK   3     ATOM PAIRS NUMBER  : 71                                          
REMARK   3     RMSD               : 0.004                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071950.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38868                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06M MAGNESIUM CHLORIDE, 0.08M MES,     
REMARK 280  1.3M SODIUM CITRATE, 2% BENZAMIDINE HYDROCHLORIDE, PH 6.0, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      110.75500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.77500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      110.75500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       63.77500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
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: D                                     
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: 5                                                       
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: E                                     
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: 6                                                       
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: F                                     
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     SER A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     THR A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     LEU A   163                                                      
REMARK 465     THR A   164                                                      
REMARK 465     GLN A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     ASN A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     LEU A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     LYS A   285                                                      
REMARK 465     MET A   286                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     ILE A   289                                                      
REMARK 465     ALA A   290                                                      
REMARK 465     VAL A   291                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     SER B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     THR B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     LEU B   163                                                      
REMARK 465     THR B   164                                                      
REMARK 465     GLN B   165                                                      
REMARK 465     THR B   166                                                      
REMARK 465     ASN B   167                                                      
REMARK 465     HIS B   168                                                      
REMARK 465     VAL B   169                                                      
REMARK 465     LEU B   170                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     LEU B   283                                                      
REMARK 465     ASP B   284                                                      
REMARK 465     LYS B   285                                                      
REMARK 465     MET B   286                                                      
REMARK 465     LYS B   287                                                      
REMARK 465     THR B   288                                                      
REMARK 465     ILE B   289                                                      
REMARK 465     ALA B   290                                                      
REMARK 465     VAL B   291                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     SER C   159                                                      
REMARK 465     GLU C   160                                                      
REMARK 465     THR C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     THR C   164                                                      
REMARK 465     GLN C   165                                                      
REMARK 465     THR C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     HIS C   168                                                      
REMARK 465     VAL C   169                                                      
REMARK 465     LEU C   170                                                      
REMARK 465     GLY C   171                                                      
REMARK 465     LEU C   283                                                      
REMARK 465     ASP C   284                                                      
REMARK 465     LYS C   285                                                      
REMARK 465     MET C   286                                                      
REMARK 465     LYS C   287                                                      
REMARK 465     THR C   288                                                      
REMARK 465     ILE C   289                                                      
REMARK 465     ALA C   290                                                      
REMARK 465     VAL C   291                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     SER D   159                                                      
REMARK 465     GLU D   160                                                      
REMARK 465     THR D   161                                                      
REMARK 465     SER D   162                                                      
REMARK 465     LEU D   163                                                      
REMARK 465     THR D   164                                                      
REMARK 465     GLN D   165                                                      
REMARK 465     THR D   166                                                      
REMARK 465     ASN D   167                                                      
REMARK 465     HIS D   168                                                      
REMARK 465     VAL D   169                                                      
REMARK 465     LEU D   170                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     ASP D   284                                                      
REMARK 465     LYS D   285                                                      
REMARK 465     MET D   286                                                      
REMARK 465     LYS D   287                                                      
REMARK 465     THR D   288                                                      
REMARK 465     ILE D   289                                                      
REMARK 465     ALA D   290                                                      
REMARK 465     VAL D   291                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     ALA E   157                                                      
REMARK 465     LEU E   158                                                      
REMARK 465     SER E   159                                                      
REMARK 465     GLU E   160                                                      
REMARK 465     THR E   161                                                      
REMARK 465     SER E   162                                                      
REMARK 465     LEU E   163                                                      
REMARK 465     THR E   164                                                      
REMARK 465     GLN E   165                                                      
REMARK 465     THR E   166                                                      
REMARK 465     ASN E   167                                                      
REMARK 465     HIS E   168                                                      
REMARK 465     VAL E   169                                                      
REMARK 465     LEU E   170                                                      
REMARK 465     GLY E   171                                                      
REMARK 465     ASP E   284                                                      
REMARK 465     LYS E   285                                                      
REMARK 465     MET E   286                                                      
REMARK 465     LYS E   287                                                      
REMARK 465     THR E   288                                                      
REMARK 465     ILE E   289                                                      
REMARK 465     ALA E   290                                                      
REMARK 465     VAL E   291                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     ALA F   157                                                      
REMARK 465     LEU F   158                                                      
REMARK 465     SER F   159                                                      
REMARK 465     GLU F   160                                                      
REMARK 465     THR F   161                                                      
REMARK 465     SER F   162                                                      
REMARK 465     LEU F   163                                                      
REMARK 465     THR F   164                                                      
REMARK 465     GLN F   165                                                      
REMARK 465     THR F   166                                                      
REMARK 465     ASN F   167                                                      
REMARK 465     HIS F   168                                                      
REMARK 465     VAL F   169                                                      
REMARK 465     LEU F   170                                                      
REMARK 465     GLY F   171                                                      
REMARK 465     ASP F   284                                                      
REMARK 465     LYS F   285                                                      
REMARK 465     MET F   286                                                      
REMARK 465     LYS F   287                                                      
REMARK 465     THR F   288                                                      
REMARK 465     ILE F   289                                                      
REMARK 465     ALA F   290                                                      
REMARK 465     VAL F   291                                                      
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     LYS A  15    CG   CD   CE   NZ                                   
REMARK 470     MET A  21    CG   SD   CE                                        
REMARK 470     LYS A  53    CG   CD   CE   NZ                                   
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 172    OG1  CG2                                            
REMARK 470     GLU A 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     LYS B  15    CG   CD   CE   NZ                                   
REMARK 470     MET B  21    CG   SD   CE                                        
REMARK 470     LYS B  53    CG   CD   CE   NZ                                   
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     ARG B 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 172    OG1  CG2                                            
REMARK 470     GLU B 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 235    CG   CD   CE   NZ                                   
REMARK 470     LYS C  15    CG   CD   CE   NZ                                   
REMARK 470     MET C  21    CG   SD   CE                                        
REMARK 470     LYS C  53    CG   CD   CE   NZ                                   
REMARK 470     ARG C 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 172    OG1  CG2                                            
REMARK 470     GLU C 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 235    CG   CD   CE   NZ                                   
REMARK 470     GLU D  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE D  42    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE D  43    CG1  CG2  CD1                                       
REMARK 470     ARG D  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  49    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  50    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  53    CG   CD   CE   NZ                                   
REMARK 470     ARG D  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  78    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 122    CG   CD   CE   NZ                                   
REMARK 470     ARG D 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 145    CG   CD   CE   NZ                                   
REMARK 470     LYS D 156    CG   CD   CE   NZ                                   
REMARK 470     LYS D 182    CG   CD   CE   NZ                                   
REMARK 470     GLU D 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 235    CG   CD   CE   NZ                                   
REMARK 470     ARG D 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 251    CG   CD   CE   NZ                                   
REMARK 470     GLU D 273    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 282    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 283    CG   CD1  CD2                                       
REMARK 470     GLU E  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE E  42    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE E  43    CG1  CG2  CD1                                       
REMARK 470     ARG E  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  50    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  53    CG   CD   CE   NZ                                   
REMARK 470     ARG E  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  78    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  79    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 145    CG   CD   CE   NZ                                   
REMARK 470     LYS E 156    CG   CD   CE   NZ                                   
REMARK 470     LYS E 182    CG   CD   CE   NZ                                   
REMARK 470     GLU E 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 235    CG   CD   CE   NZ                                   
REMARK 470     ARG E 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 251    CG   CD   CE   NZ                                   
REMARK 470     GLU E 273    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 280    CG1  CG2                                            
REMARK 470     GLU E 282    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 283    CG   CD1  CD2                                       
REMARK 470     GLU F  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE F  42    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE F  43    CG1  CG2  CD1                                       
REMARK 470     ARG F  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  48    CG   CD   CE   NZ                                   
REMARK 470     GLU F  49    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  50    CG   CD   OE1  OE2                                  
REMARK 470     THR F  51    OG1  CG2                                            
REMARK 470     LYS F  53    CG   CD   CE   NZ                                   
REMARK 470     ARG F  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  78    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  79    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 145    CG   CD   CE   NZ                                   
REMARK 470     LYS F 156    CG   CD   CE   NZ                                   
REMARK 470     LYS F 182    CG   CD   CE   NZ                                   
REMARK 470     GLU F 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 235    CG   CD   CE   NZ                                   
REMARK 470     ARG F 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 251    CG   CD   CE   NZ                                   
REMARK 470     GLU F 273    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 280    CG1  CG2                                            
REMARK 470     GLU F 282    CG   CD   OE1  OE2                                  
REMARK 470     LEU F 283    CG   CD1  CD2                                       
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    GLU A   8     -121.54     53.02                                   
REMARK 500    ASP A  81       11.71     54.56                                   
REMARK 500    GLU A 212     -137.64     53.78                                   
REMARK 500    GLN A 223      -72.26   -102.11                                   
REMARK 500    ARG A 234       67.01     60.56                                   
REMARK 500    GLU B   8     -123.37     52.39                                   
REMARK 500    LEU B  52      -30.32    -39.58                                   
REMARK 500    GLU B  79      -62.54   -105.48                                   
REMARK 500    ARG B 132       -2.98     64.11                                   
REMARK 500    VAL B 173        6.11     55.28                                   
REMARK 500    GLU B 212     -134.35     55.61                                   
REMARK 500    GLN B 223      -63.61   -103.83                                   
REMARK 500    ARG B 234       64.91     61.05                                   
REMARK 500    GLU C   8     -116.23     54.52                                   
REMARK 500    ARG C 132       11.40     56.87                                   
REMARK 500    VAL C 173        9.40     54.63                                   
REMARK 500    GLU C 212     -137.45     56.20                                   
REMARK 500    GLN C 223      -72.31   -102.02                                   
REMARK 500    ARG C 234       60.41     62.21                                   
REMARK 500    LYS C 235      -11.75    -48.26                                   
REMARK 500    GLU D   8     -115.54     62.36                                   
REMARK 500    VAL D  13      -51.23   -124.91                                   
REMARK 500    ILE D  31      -68.77   -103.32                                   
REMARK 500    ASP D  80        2.20     83.74                                   
REMARK 500    ARG D 132       -3.80     79.45                                   
REMARK 500    PRO D 208       38.36    -77.19                                   
REMARK 500    ILE D 222     -123.03     53.72                                   
REMARK 500    ASP D 232      -75.24    -99.32                                   
REMARK 500    GLU E   8     -126.54     60.54                                   
REMARK 500    VAL E  13      -75.13   -119.03                                   
REMARK 500    ILE E  31      -72.43   -105.89                                   
REMARK 500    ARG E 132       -8.50     71.84                                   
REMARK 500    ALA E 155     -123.12     47.37                                   
REMARK 500    ILE E 222     -123.20     53.60                                   
REMARK 500    VAL E 233     -166.20   -100.63                                   
REMARK 500    GLU F   8     -130.70     57.94                                   
REMARK 500    VAL F  13      -78.75   -118.53                                   
REMARK 500    ILE F  31      -61.50    -97.72                                   
REMARK 500    ARG F 132      -11.20     72.79                                   
REMARK 500    ALA F 155     -124.71     50.49                                   
REMARK 500    PRO F 208       40.08    -78.27                                   
REMARK 500    ILE F 222     -123.13     53.76                                   
REMARK 500    ASP F 232      -71.18   -100.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ANP A  300                                                       
REMARK 610     ANP B  300                                                       
REMARK 610     ANP C  300                                                       
REMARK 610     ANP D  300                                                       
REMARK 610     ANP E  300                                                       
REMARK 610     ANP F  300                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP D 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP F 300                 
DBREF  4EQM A    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
DBREF  4EQM B    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
DBREF  4EQM C    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
DBREF  4EQM D    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
DBREF  4EQM E    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
DBREF  4EQM F    1   291  UNP    Q7A5Z8   Q7A5Z8_STAAN     1    291             
SEQADV 4EQM GLY A   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER A   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS A    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM GLY B   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER B   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS B    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM GLY C   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER C   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS C    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM GLY D   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER D   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS D    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM GLY E   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER E   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS E    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM GLY F   -2  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM SER F   -1  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQADV 4EQM HIS F    0  UNP  Q7A5Z8              EXPRESSION TAG                 
SEQRES   1 A  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 A  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 A  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 A  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 A  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 A  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 A  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 A  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 A  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 A  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 A  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 A  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 A  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 A  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 A  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 A  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 A  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 A  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 A  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 A  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 A  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 A  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 A  294  ASP LYS MET LYS THR ILE ALA VAL                              
SEQRES   1 B  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 B  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 B  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 B  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 B  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 B  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 B  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 B  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 B  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 B  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 B  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 B  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 B  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 B  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 B  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 B  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 B  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 B  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 B  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 B  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 B  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 B  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 B  294  ASP LYS MET LYS THR ILE ALA VAL                              
SEQRES   1 C  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 C  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 C  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 C  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 C  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 C  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 C  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 C  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 C  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 C  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 C  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 C  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 C  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 C  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 C  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 C  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 C  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 C  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 C  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 C  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 C  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 C  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 C  294  ASP LYS MET LYS THR ILE ALA VAL                              
SEQRES   1 D  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 D  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 D  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 D  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 D  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 D  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 D  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 D  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 D  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 D  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 D  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 D  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 D  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 D  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 D  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 D  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 D  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 D  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 D  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 D  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 D  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 D  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 D  294  ASP LYS MET LYS THR ILE ALA VAL                              
SEQRES   1 E  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 E  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 E  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 E  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 E  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 E  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 E  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 E  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 E  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 E  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 E  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 E  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 E  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 E  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 E  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 E  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 E  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 E  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 E  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 E  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 E  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 E  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 E  294  ASP LYS MET LYS THR ILE ALA VAL                              
SEQRES   1 F  294  GLY SER HIS MET ILE GLY LYS ILE ILE ASN GLU ARG TYR          
SEQRES   2 F  294  LYS ILE VAL ASP LYS LEU GLY GLY GLY GLY MET SER THR          
SEQRES   3 F  294  VAL TYR LEU ALA GLU ASP THR ILE LEU ASN ILE LYS VAL          
SEQRES   4 F  294  ALA ILE LYS ALA ILE PHE ILE PRO PRO ARG GLU LYS GLU          
SEQRES   5 F  294  GLU THR LEU LYS ARG PHE GLU ARG GLU VAL HIS ASN SER          
SEQRES   6 F  294  SER GLN LEU SER HIS GLN ASN ILE VAL SER MET ILE ASP          
SEQRES   7 F  294  VAL ASP GLU GLU ASP ASP CYS TYR TYR LEU VAL MET GLU          
SEQRES   8 F  294  TYR ILE GLU GLY PRO THR LEU SER GLU TYR ILE GLU SER          
SEQRES   9 F  294  HIS GLY PRO LEU SER VAL ASP THR ALA ILE ASN PHE THR          
SEQRES  10 F  294  ASN GLN ILE LEU ASP GLY ILE LYS HIS ALA HIS ASP MET          
SEQRES  11 F  294  ARG ILE VAL HIS ARG ASP ILE LYS PRO GLN ASN ILE LEU          
SEQRES  12 F  294  ILE ASP SER ASN LYS THR LEU LYS ILE PHE ASP PHE GLY          
SEQRES  13 F  294  ILE ALA LYS ALA LEU SER GLU THR SER LEU THR GLN THR          
SEQRES  14 F  294  ASN HIS VAL LEU GLY THR VAL GLN TYR PHE SER PRO GLU          
SEQRES  15 F  294  GLN ALA LYS GLY GLU ALA THR ASP GLU CYS THR ASP ILE          
SEQRES  16 F  294  TYR SER ILE GLY ILE VAL LEU TYR GLU MET LEU VAL GLY          
SEQRES  17 F  294  GLU PRO PRO PHE ASN GLY GLU THR ALA VAL SER ILE ALA          
SEQRES  18 F  294  ILE LYS HIS ILE GLN ASP SER VAL PRO ASN VAL THR THR          
SEQRES  19 F  294  ASP VAL ARG LYS ASP ILE PRO GLN SER LEU SER ASN VAL          
SEQRES  20 F  294  ILE LEU ARG ALA THR GLU LYS ASP LYS ALA ASN ARG TYR          
SEQRES  21 F  294  LYS THR ILE GLN GLU MET LYS ASP ASP LEU SER SER VAL          
SEQRES  22 F  294  LEU HIS GLU ASN ARG ALA ASN GLU ASP VAL TYR GLU LEU          
SEQRES  23 F  294  ASP LYS MET LYS THR ILE ALA VAL                              
HET    ANP  A 300      27                                                       
HET    BEN  A 301       9                                                       
HET    ANP  B 300      27                                                       
HET    BEN  B 301       9                                                       
HET    ANP  C 300      27                                                       
HET    BEN  C 301       9                                                       
HET    ANP  D 300      27                                                       
HET    ANP  E 300      27                                                       
HET    ANP  F 300      27                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   7  ANP    6(C10 H17 N6 O12 P3)                                         
FORMUL   8  BEN    3(C7 H8 N2)                                                  
HELIX    1   1 LYS A   48  SER A   63  1                                  16    
HELIX    2   2 THR A   94  GLY A  103  1                                  10    
HELIX    3   3 SER A  106  MET A  127  1                                  22    
HELIX    4   4 SER A  177  GLY A  183  1                                   7    
HELIX    5   5 CYS A  189  GLY A  205  1                                  17    
HELIX    6   6 THR A  213  GLN A  223  1                                  11    
HELIX    7   7 ASN A  228  VAL A  233  1                                   6    
HELIX    8   8 PRO A  238  THR A  249  1                                  12    
HELIX    9   9 ASP A  252  ARG A  256  5                                   5    
HELIX   10  10 THR A  259  SER A  269  1                                  11    
HELIX   11  11 LYS B   48  SER B   63  1                                  16    
HELIX   12  12 THR B   94  GLY B  103  1                                  10    
HELIX   13  13 SER B  106  MET B  127  1                                  22    
HELIX   14  14 LYS B  135  GLN B  137  5                                   3    
HELIX   15  15 SER B  177  GLY B  183  1                                   7    
HELIX   16  16 CYS B  189  GLY B  205  1                                  17    
HELIX   17  17 THR B  213  GLN B  223  1                                  11    
HELIX   18  18 ASN B  228  VAL B  233  1                                   6    
HELIX   19  19 PRO B  238  THR B  249  1                                  12    
HELIX   20  20 ASP B  252  ARG B  256  5                                   5    
HELIX   21  21 THR B  259  SER B  269  1                                  11    
HELIX   22  22 LYS C   48  SER C   63  1                                  16    
HELIX   23  23 THR C   94  GLY C  103  1                                  10    
HELIX   24  24 SER C  106  MET C  127  1                                  22    
HELIX   25  25 SER C  177  GLY C  183  1                                   7    
HELIX   26  26 CYS C  189  GLY C  205  1                                  17    
HELIX   27  27 THR C  213  GLN C  223  1                                  11    
HELIX   28  28 ASN C  228  VAL C  233  1                                   6    
HELIX   29  29 PRO C  238  THR C  249  1                                  12    
HELIX   30  30 THR C  259  SER C  269  1                                  11    
HELIX   31  31 THR D   51  SER D   63  1                                  13    
HELIX   32  32 GLU D   78  ASP D   80  5                                   3    
HELIX   33  33 THR D   94  HIS D  102  1                                   9    
HELIX   34  34 ASP D  108  MET D  127  1                                  20    
HELIX   35  35 THR D  172  PHE D  176  5                                   5    
HELIX   36  36 SER D  177  GLY D  183  1                                   7    
HELIX   37  37 GLU D  188  GLY D  205  1                                  18    
HELIX   38  38 THR D  213  HIS D  221  1                                   9    
HELIX   39  39 ASN D  228  VAL D  233  1                                   6    
HELIX   40  40 SER D  240  THR D  249  1                                  10    
HELIX   41  41 THR D  259  VAL D  270  1                                  12    
HELIX   42  42 LYS E   48  SER E   63  1                                  16    
HELIX   43  43 THR E   94  HIS E  102  1                                   9    
HELIX   44  44 ASP E  108  MET E  127  1                                  20    
HELIX   45  45 THR E  172  PHE E  176  5                                   5    
HELIX   46  46 SER E  177  GLY E  183  1                                   7    
HELIX   47  47 GLU E  188  GLY E  205  1                                  18    
HELIX   48  48 THR E  213  HIS E  221  1                                   9    
HELIX   49  49 ASN E  228  VAL E  233  1                                   6    
HELIX   50  50 SER E  240  THR E  249  1                                  10    
HELIX   51  51 THR E  259  VAL E  270  1                                  12    
HELIX   52  52 LYS F   48  SER F   63  1                                  16    
HELIX   53  53 THR F   94  HIS F  102  1                                   9    
HELIX   54  54 ASP F  108  MET F  127  1                                  20    
HELIX   55  55 THR F  172  PHE F  176  5                                   5    
HELIX   56  56 SER F  177  GLY F  183  1                                   7    
HELIX   57  57 GLU F  188  GLY F  205  1                                  18    
HELIX   58  58 THR F  213  HIS F  221  1                                   9    
HELIX   59  59 ASN F  228  VAL F  233  1                                   6    
HELIX   60  60 SER F  240  THR F  249  1                                  10    
HELIX   61  61 THR F  259  VAL F  270  1                                  12    
SHEET    1   A 6 ILE A   6  ASN A   7  0                                        
SHEET    2   A 6 TYR A  10  GLY A  19 -1  O  TYR A  10   N  ASN A   7           
SHEET    3   A 6 SER A  22  ASP A  29 -1  O  SER A  22   N  GLY A  19           
SHEET    4   A 6 LYS A  35  PHE A  42 -1  O  ALA A  40   N  THR A  23           
SHEET    5   A 6 CYS A  82  GLU A  88 -1  O  MET A  87   N  ALA A  37           
SHEET    6   A 6 MET A  73  GLU A  78 -1  N  ASP A  77   O  TYR A  84           
SHEET    1   B 2 ILE A 139  ILE A 141  0                                        
SHEET    2   B 2 LEU A 147  ILE A 149 -1  O  LYS A 148   N  LEU A 140           
SHEET    1   C 6 ILE B   6  ASN B   7  0                                        
SHEET    2   C 6 TYR B  10  GLY B  19 -1  O  TYR B  10   N  ASN B   7           
SHEET    3   C 6 SER B  22  ASP B  29 -1  O  SER B  22   N  GLY B  19           
SHEET    4   C 6 LYS B  35  PHE B  42 -1  O  ALA B  40   N  THR B  23           
SHEET    5   C 6 CYS B  82  GLU B  88 -1  O  MET B  87   N  ALA B  37           
SHEET    6   C 6 MET B  73  GLU B  78 -1  N  ASP B  77   O  TYR B  84           
SHEET    1   D 2 ILE B 139  ILE B 141  0                                        
SHEET    2   D 2 LEU B 147  ILE B 149 -1  O  LYS B 148   N  LEU B 140           
SHEET    1   E 6 ILE C   6  ASN C   7  0                                        
SHEET    2   E 6 TYR C  10  GLY C  19 -1  O  TYR C  10   N  ASN C   7           
SHEET    3   E 6 SER C  22  ASP C  29 -1  O  SER C  22   N  GLY C  19           
SHEET    4   E 6 LYS C  35  PHE C  42 -1  O  ALA C  40   N  THR C  23           
SHEET    5   E 6 CYS C  82  GLU C  88 -1  O  MET C  87   N  ALA C  37           
SHEET    6   E 6 MET C  73  GLU C  78 -1  N  ASP C  77   O  TYR C  84           
SHEET    1   F 2 ILE C 139  ILE C 141  0                                        
SHEET    2   F 2 LEU C 147  ILE C 149 -1  O  LYS C 148   N  LEU C 140           
SHEET    1   G 6 ILE D   6  ASN D   7  0                                        
SHEET    2   G 6 TYR D  10  GLY D  19 -1  O  TYR D  10   N  ASN D   7           
SHEET    3   G 6 SER D  22  ASP D  29 -1  O  LEU D  26   N  VAL D  13           
SHEET    4   G 6 LYS D  35  PHE D  42 -1  O  ALA D  40   N  THR D  23           
SHEET    5   G 6 CYS D  82  GLU D  88 -1  O  MET D  87   N  ALA D  37           
SHEET    6   G 6 MET D  73  ASP D  77 -1  N  ASP D  75   O  VAL D  86           
SHEET    1   H 2 ILE D 139  ILE D 141  0                                        
SHEET    2   H 2 LEU D 147  ILE D 149 -1  O  LYS D 148   N  LEU D 140           
SHEET    1   I 6 ILE E   6  ASN E   7  0                                        
SHEET    2   I 6 TYR E  10  GLY E  19 -1  O  TYR E  10   N  ASN E   7           
SHEET    3   I 6 SER E  22  ASP E  29 -1  O  LEU E  26   N  VAL E  13           
SHEET    4   I 6 LYS E  35  PHE E  42 -1  O  ALA E  40   N  THR E  23           
SHEET    5   I 6 CYS E  82  GLU E  88 -1  O  MET E  87   N  ALA E  37           
SHEET    6   I 6 MET E  73  ASP E  77 -1  N  ASP E  75   O  VAL E  86           
SHEET    1   J 2 ILE E 139  ILE E 141  0                                        
SHEET    2   J 2 LEU E 147  ILE E 149 -1  O  LYS E 148   N  LEU E 140           
SHEET    1   K 6 ILE F   6  ASN F   7  0                                        
SHEET    2   K 6 TYR F  10  GLY F  19 -1  O  TYR F  10   N  ASN F   7           
SHEET    3   K 6 SER F  22  ASP F  29 -1  O  LEU F  26   N  VAL F  13           
SHEET    4   K 6 LYS F  35  PHE F  42 -1  O  ALA F  40   N  THR F  23           
SHEET    5   K 6 CYS F  82  GLU F  88 -1  O  TYR F  83   N  ILE F  41           
SHEET    6   K 6 MET F  73  ASP F  77 -1  N  ASP F  75   O  VAL F  86           
SHEET    1   L 2 ILE F 139  ILE F 141  0                                        
SHEET    2   L 2 LEU F 147  ILE F 149 -1  O  LYS F 148   N  LEU F 140           
CISPEP   1 PRO A   45    ARG A   46          0        15.32                     
CISPEP   2 PRO B   45    ARG B   46          0        26.58                     
CISPEP   3 PRO C   45    ARG C   46          0        14.70                     
SITE     1 AC1  8 LEU A  16  LYS A  39  MET A  87  GLU A  88                    
SITE     2 AC1  8 TYR A  89  ILE A  90  LEU A 140  PHE A 150                    
SITE     1 AC2  6 SER A  63  GLN A  64  LEU A  65  SER A  66                    
SITE     2 AC2  6 MET A  73  GLU C  88                                          
SITE     1 AC3  8 LEU B  16  GLY B  18  LYS B  39  GLU B  88                    
SITE     2 AC3  8 TYR B  89  ILE B  90  LEU B 140  PHE B 150                    
SITE     1 AC4  5 SER B  63  LEU B  65  SER B  66  MET B  73                    
SITE     2 AC4  5 GLU B  88                                                     
SITE     1 AC5  7 LEU C  16  GLY C  18  LYS C  39  GLU C  88                    
SITE     2 AC5  7 TYR C  89  ILE C  90  LEU C 140                               
SITE     1 AC6  6 GLU A  88  SER C  63  GLN C  64  LEU C  65                    
SITE     2 AC6  6 SER C  66  MET C  73                                          
SITE     1 AC7  8 SER D  22  VAL D  24  GLU D  88  TYR D  89                    
SITE     2 AC7  8 ILE D  90  LEU D 140  PHE D 150  ASP D 151                    
SITE     1 AC8  8 VAL E  24  LYS E  39  GLU E  88  TYR E  89                    
SITE     2 AC8  8 ILE E  90  LYS E 135  LEU E 140  PHE E 150                    
SITE     1 AC9  8 VAL F  24  LYS F  39  GLU F  88  TYR F  89                    
SITE     2 AC9  8 ILE F  90  LYS F 135  LEU F 140  PHE F 150                    
CRYST1  221.510  127.550   70.280  90.00  89.96  90.00 C 1 2 1      24          
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      0.004514  0.000000 -0.000003        0.00000                         
SCALE2      0.000000  0.007840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014229        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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