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Database: PDB
Entry: 6G4J
LinkDB: 6G4J
Original site: 6G4J 
HEADER    TRANSFERASE                             27-MAR-18   6G4J              
TITLE     STRUCTURE OF THE PROTEIN KINASE YABT FROM BACILLUS SUBTILIS IN COMPLEX
TITLE    2 WITH AN ALPHAREP CRYSTALLIZATION HELPER                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE SERINE/THREONINE-PROTEIN KINASE YABT;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.11.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: THE C-TERMINAL TRANSMEMBRANE HELIX OF YABT (RESIDUES  
COMPND   7 316-338) HAS BEEN DELETED. THE JUXTAMEMBRANE REGION (RESIDUES 274-   
COMPND   8 315) IS DISORDERED.;                                                 
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ALPHAREP BE8;                                              
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: THE N-TERMINAL HIS-TAG AND THE C-TERMINAL LINKER ARE  
COMPND  14 DISORDERED.                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: YABT, BSU00660;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BACTERIAL HANKS-TYPE PROTEIN KINASE, COMPLEX WITH AN ARTIFICIAL       
KEYWDS   2 BINDER, SIGNALING PROTEIN, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.NESSLER,A.CAVAGNINO,J.L.RABEFIRAISANA                               
REVDAT   2   06-FEB-19 6G4J    1       JRNL                                     
REVDAT   1   30-JAN-19 6G4J    0                                                
JRNL        AUTH   L.SHI,A.CAVAGNINO,J.L.RABEFIRAISANA,N.LAZAR,                 
JRNL        AUTH 2 I.LI DE LA SIERRA-GALLAY,F.OCHSENBEIN,M.VALERIO-LEPINIEC,    
JRNL        AUTH 3 A.URVOAS,P.MINARD,I.MIJAKOVIC,S.NESSLER                      
JRNL        TITL   STRUCTURAL ANALYSIS OF THE HANKS-TYPE PROTEIN KINASE YABT    
JRNL        TITL 2 FROMBACILLUS SUBTILISPROVIDES NEW INSIGHTS IN ITS            
JRNL        TITL 3 DNA-DEPENDENT ACTIVATION.                                    
JRNL        REF    FRONT MICROBIOL               V.   9  3014 2018              
JRNL        REFN                   ESSN 1664-302X                               
JRNL        PMID   30671027                                                     
JRNL        DOI    10.3389/FMICB.2018.03014                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 56281                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2814                            
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 40.5257 -  4.3382    0.99     2879   152  0.1596 0.1535        
REMARK   3     2  4.3382 -  3.4439    0.99     2726   144  0.1609 0.2021        
REMARK   3     3  3.4439 -  3.0088    0.99     2709   142  0.1879 0.2376        
REMARK   3     4  3.0088 -  2.7337    1.00     2703   142  0.1969 0.2292        
REMARK   3     5  2.7337 -  2.5378    1.00     2688   142  0.1956 0.2152        
REMARK   3     6  2.5378 -  2.3882    0.99     2703   142  0.1950 0.2415        
REMARK   3     7  2.3882 -  2.2686    1.00     2669   141  0.1920 0.2239        
REMARK   3     8  2.2686 -  2.1699    0.99     2653   138  0.1905 0.2103        
REMARK   3     9  2.1699 -  2.0863    1.00     2670   141  0.1931 0.2375        
REMARK   3    10  2.0863 -  2.0144    1.00     2640   139  0.1979 0.2075        
REMARK   3    11  2.0144 -  1.9514    1.00     2677   141  0.2031 0.2434        
REMARK   3    12  1.9514 -  1.8956    0.99     2646   139  0.2198 0.2575        
REMARK   3    13  1.8956 -  1.8457    1.00     2650   139  0.2127 0.2646        
REMARK   3    14  1.8457 -  1.8007    1.00     2650   140  0.2272 0.2620        
REMARK   3    15  1.8007 -  1.7597    1.00     2647   139  0.2341 0.2563        
REMARK   3    16  1.7597 -  1.7223    1.00     2663   140  0.2586 0.2903        
REMARK   3    17  1.7223 -  1.6878    1.00     2622   138  0.2646 0.3013        
REMARK   3    18  1.6878 -  1.6560    1.00     2654   140  0.2748 0.3000        
REMARK   3    19  1.6560 -  1.6264    1.00     2628   138  0.2832 0.3026        
REMARK   3    20  1.6264 -  1.5988    0.97     2590   137  0.2865 0.3144        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.180           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3140                                  
REMARK   3   ANGLE     :  1.017           4247                                  
REMARK   3   CHIRALITY :  0.037            474                                  
REMARK   3   PLANARITY :  0.005            545                                  
REMARK   3   DIHEDRAL  : 11.916           1190                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6G4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009407.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56285                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.599                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.280                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HEPES,, PH 7.5, VAPOR          
REMARK 280  DIFFUSION, TEMPERATURE 291K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       33.84500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.43500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.84500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.43500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   274                                                      
REMARK 465     LYS A   275                                                      
REMARK 465     GLN A   276                                                      
REMARK 465     PRO A   277                                                      
REMARK 465     ILE A   278                                                      
REMARK 465     LYS A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     SER A   281                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     GLN A   283                                                      
REMARK 465     PRO A   284                                                      
REMARK 465     ALA A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     ARG A   287                                                      
REMARK 465     GLN A   288                                                      
REMARK 465     ARG A   289                                                      
REMARK 465     GLN A   290                                                      
REMARK 465     GLN A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     PRO A   293                                                      
REMARK 465     ARG A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     LYS A   297                                                      
REMARK 465     ILE A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     LYS A   300                                                      
REMARK 465     THR A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     TYR A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     LYS A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ALA A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     GLY A   314                                                      
REMARK 465     LEU A   315                                                      
REMARK 465     MET B    -9                                                      
REMARK 465     ARG B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     THR B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     LEU B   127                                                      
REMARK 465     ILE B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     GLY B   130                                                      
REMARK 465     GLY B   131                                                      
REMARK 465     GLY B   132                                                      
REMARK 465     GLY B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   514     O    HOH A   555              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A   2      -53.43   -136.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6G4J A    1   315  UNP    P37562   PKN1_BACSU       1    315             
DBREF  6G4J B   -9   138  PDB    6G4J     6G4J            -9    138             
SEQRES   1 A  315  MET MET ASN ASP ALA LEU THR SER LEU ALA CYS SER LEU          
SEQRES   2 A  315  LYS PRO GLY THR THR ILE LYS GLY LYS TRP ASN GLY ASN          
SEQRES   3 A  315  THR TYR THR LEU ARG LYS GLN LEU GLY LYS GLY ALA ASN          
SEQRES   4 A  315  GLY ILE VAL TYR LEU ALA GLU THR SER ASP GLY HIS VAL          
SEQRES   5 A  315  ALA LEU LYS VAL SER ASP ASP SER LEU SER ILE THR SER          
SEQRES   6 A  315  GLU VAL ASN VAL LEU LYS SER PHE SER LYS ALA GLN SER          
SEQRES   7 A  315  VAL THR MET GLY PRO SER PHE PHE ASP THR ASP ASP ALA          
SEQRES   8 A  315  TYR ILE PRO SER ALA ASN THR LYS VAL SER PHE TYR ALA          
SEQRES   9 A  315  MET GLU TYR ILE LYS GLY PRO LEU LEU LEU LYS TYR VAL          
SEQRES  10 A  315  SER ASP LYS GLY ALA GLU TRP ILE PRO VAL LEU MET ILE          
SEQRES  11 A  315  GLN LEU LEU SER SER LEU SER VAL LEU HIS GLN GLN GLY          
SEQRES  12 A  315  TRP ILE PHE GLY ASP LEU LYS PRO ASP ASN LEU ILE VAL          
SEQRES  13 A  315  THR GLY PRO PRO ALA ARG ILE ARG CYS ILE ASP VAL GLY          
SEQRES  14 A  315  GLY THR THR LYS GLU GLY ARG ALA ILE LYS GLU TYR THR          
SEQRES  15 A  315  GLU PHE TYR ASP ARG GLY TYR TRP GLY TYR GLY THR ARG          
SEQRES  16 A  315  LYS ALA GLU PRO SER TYR ASP LEU PHE ALA VAL ALA MET          
SEQRES  17 A  315  ILE MET ILE ASN SER VAL HIS LYS LYS GLU PHE LYS LYS          
SEQRES  18 A  315  THR ASN GLN PRO LYS GLU GLN LEU ARG SER LEU ILE GLU          
SEQRES  19 A  315  GLY ASN PRO LEU LEU GLN LYS TYR LYS LYS ALA LEU PHE          
SEQRES  20 A  315  SER ALA LEU ASN GLY ASP TYR GLN SER ALA ASP GLU MET          
SEQRES  21 A  315  LYS LYS ASP MET LEU ASP ALA GLY GLN LYS ALA ALA GLN          
SEQRES  22 A  315  ARG LYS GLN PRO ILE LYS ALA SER PRO GLN PRO ALA THR          
SEQRES  23 A  315  ARG GLN ARG GLN GLN LYS PRO ARG GLN GLY LYS ILE THR          
SEQRES  24 A  315  LYS THR ARG TYR THR PRO LYS GLN LYS PRO ALA LYS SER          
SEQRES  25 A  315  GLY GLY LEU                                                  
SEQRES   1 B  148  MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO          
SEQRES   2 B  148  GLU LYS VAL GLU MET TYR ILE LYS ASN LEU GLN ASP ASP          
SEQRES   3 B  148  SER ALA VAL VAL ARG ASP TYR ALA ALA ALA ALA LEU GLY          
SEQRES   4 B  148  LYS ILE GLY ASP GLU ARG ALA VAL GLU PRO LEU ILE LYS          
SEQRES   5 B  148  ALA LEU LYS ASP GLU ASP GLU TYR VAL ARG GLN SER ALA          
SEQRES   6 B  148  ALA TRP ALA LEU GLY GLU ILE GLY ASP GLU ARG ALA VAL          
SEQRES   7 B  148  GLU PRO LEU ILE LYS ALA LEU LYS ASP GLU ASP PRO SER          
SEQRES   8 B  148  VAL ARG LEU THR ALA ALA GLU ALA LEU GLY GLN ILE GLY          
SEQRES   9 B  148  GLY GLU ARG VAL ARG ALA ALA MET GLU LYS LEU ALA GLU          
SEQRES  10 B  148  THR GLY THR GLY PHE ALA ARG LYS VAL ALA VAL ASN TYR          
SEQRES  11 B  148  LEU GLU THR HIS LYS SER LEU ILE SER GLY GLY GLY GLY          
SEQRES  12 B  148  SER GLY GLY GLY GLY                                          
FORMUL   3  HOH   *227(H2 O)                                                    
HELIX    1 AA1 ASN A    3  LEU A   13  1                                  11    
HELIX    2 AA2 ASP A   59  LYS A   75  1                                  17    
HELIX    3 AA3 LEU A  112  GLY A  121  1                                  10    
HELIX    4 AA4 GLU A  123  GLN A  142  1                                  20    
HELIX    5 AA5 LYS A  150  ASP A  152  5                                   3    
HELIX    6 AA6 THR A  182  ASP A  186  5                                   5    
HELIX    7 AA7 GLU A  198  LYS A  216  1                                  19    
HELIX    8 AA8 GLN A  224  GLY A  235  1                                  12    
HELIX    9 AA9 ASN A  236  TYR A  242  1                                   7    
HELIX   10 AB1 TYR A  242  GLY A  252  1                                  11    
HELIX   11 AB2 SER A  256  GLN A  273  1                                  18    
HELIX   12 AB3 GLU B    4  LEU B   13  1                                  10    
HELIX   13 AB4 SER B   17  GLY B   32  1                                  16    
HELIX   14 AB5 ASP B   33  ARG B   35  5                                   3    
HELIX   15 AB6 ALA B   36  LEU B   44  1                                   9    
HELIX   16 AB7 ASP B   48  GLY B   63  1                                  16    
HELIX   17 AB8 ASP B   64  ARG B   66  5                                   3    
HELIX   18 AB9 ALA B   67  ALA B   74  1                                   8    
HELIX   19 AC1 LEU B   75  ASP B   77  5                                   3    
HELIX   20 AC2 ASP B   79  GLY B   94  1                                  16    
HELIX   21 AC3 GLY B   95  GLY B  109  1                                  15    
HELIX   22 AC4 THR B  110  THR B  123  1                                  14    
SHEET    1 AA1 6 THR A  18  LYS A  20  0                                        
SHEET    2 AA1 6 THR A  27  GLY A  37 -1  O  TYR A  28   N  ILE A  19           
SHEET    3 AA1 6 GLY A  40  THR A  47 -1  O  LEU A  44   N  ARG A  31           
SHEET    4 AA1 6 GLY A  50  SER A  57 -1  O  GLY A  50   N  THR A  47           
SHEET    5 AA1 6 THR A  98  MET A 105 -1  O  MET A 105   N  ALA A  53           
SHEET    6 AA1 6 PHE A  85  ILE A  93 -1  N  ALA A  91   O  VAL A 100           
SHEET    1 AA2 2 TRP A 144  ILE A 145  0                                        
SHEET    2 AA2 2 THR A 172  LYS A 173 -1  O  THR A 172   N  ILE A 145           
SHEET    1 AA3 2 LEU A 154  THR A 157  0                                        
SHEET    2 AA3 2 ARG A 162  CYS A 165 -1  O  ARG A 164   N  ILE A 155           
CISPEP   1 GLY A  158    PRO A  159          0         0.60                     
CISPEP   2 PRO A  159    PRO A  160          0        -0.73                     
CRYST1   67.690  122.870   50.570  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014773  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008139  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019775        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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