GenomeNet

Database: PDB
Entry: 6CZ5
LinkDB: 6CZ5
Original site: 6CZ5 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-APR-18   6CZ5              
TITLE     CRYSTAL STRUCTURE OF SMALL MOLECULE AMP-ACRYLAMIDE COVALENTLY BOUND TO
TITLE    2 DDX3 S228C                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 132-607;                                      
COMPND   5 SYNONYM: DEAD BOX PROTEIN 3, X-CHROMOSOMAL, DEAD BOX, X ISOFORM,     
COMPND   6 HELICASE-LIKE PROTEIN 2, HLP2;                                       
COMPND   7 EC: 3.6.4.13;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDX3X, DBX, DDX3;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    INHIBITOR, DEAD-BOX PROTEIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.J.BARKOVICH,M.K.MOORE,Q.HU,K.M.SHOKAT                               
REVDAT   5   04-DEC-19 6CZ5    1       REMARK                                   
REVDAT   4   10-OCT-18 6CZ5    1       JRNL                                     
REVDAT   3   29-AUG-18 6CZ5    1       JRNL                                     
REVDAT   2   15-AUG-18 6CZ5    1       JRNL                                     
REVDAT   1   08-AUG-18 6CZ5    0                                                
JRNL        AUTH   K.J.BARKOVICH,M.K.MOORE,Q.HU,K.M.SHOKAT                      
JRNL        TITL   CHEMICAL GENETIC INHIBITION OF DEAD-BOX PROTEINS USING       
JRNL        TITL 2 COVALENT COMPLEMENTARITY.                                    
JRNL        REF    NUCLEIC ACIDS RES.            V.  46  8689 2018              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   30102385                                                     
JRNL        DOI    10.1093/NAR/GKY706                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12082                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.680                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 566                             
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 73.0751 -  4.7622    1.00     2999   157  0.2014 0.2392        
REMARK   3     2  4.7622 -  3.7799    1.00     2874   143  0.2036 0.2515        
REMARK   3     3  3.7799 -  3.3021    1.00     2835   125  0.2523 0.3329        
REMARK   3     4  3.3021 -  3.0002    1.00     2808   141  0.3211 0.3526        
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)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 87.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.55                          
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      :  0.002           3471                                  
REMARK   3   ANGLE     :  0.523           4692                                  
REMARK   3   CHIRALITY :  0.041            521                                  
REMARK   3   PLANARITY :  0.004            610                                  
REMARK   3   DIHEDRAL  : 10.629           2122                                  
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 6CZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233758.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12100                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.054                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
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) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.08900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 5E7J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, 8% PEG3000, PH    
REMARK 280  5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.98000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.84500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.54500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.84500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.54500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 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   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     PHE A   130                                                      
REMARK 465     THR A   131                                                      
REMARK 465     ASP A   132                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     ILE A   158                                                      
REMARK 465     ASN A   159                                                      
REMARK 465     PHE A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ARG A   259                                                      
REMARK 465     TYR A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ARG A   263                                                      
REMARK 465     TYR A   576                                                      
REMARK 465     GLU A   577                                                      
REMARK 465     HIS A   578                                                      
REMARK 465     HIS A   579                                                      
REMARK 465     TYR A   580                                                      
REMARK 465     LYS A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     SER A   583                                                      
REMARK 465     SER A   584                                                      
REMARK 465     ARG A   585                                                      
REMARK 465     GLY A   586                                                      
REMARK 465     ARG A   587                                                      
REMARK 465     SER A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     SER A   590                                                      
REMARK 465     SER A   591                                                      
REMARK 465     ARG A   592                                                      
REMARK 465     PHE A   593                                                      
REMARK 465     SER A   594                                                      
REMARK 465     GLY A   595                                                      
REMARK 465     GLY A   596                                                      
REMARK 465     PHE A   597                                                      
REMARK 465     GLY A   598                                                      
REMARK 465     ALA A   599                                                      
REMARK 465     ARG A   600                                                      
REMARK 465     ASP A   601                                                      
REMARK 465     TYR A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     GLN A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     SER A   606                                                      
REMARK 465     GLY A   607                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 163     -145.04   -104.56                                   
REMARK 500    ASP A 164      -98.20   -125.53                                   
REMARK 500    THR A 201      -78.76   -107.89                                   
REMARK 500    THR A 226       47.00    -91.04                                   
REMARK 500    PHE A 385       62.72   -159.31                                   
REMARK 500    THR A 411       92.48     57.88                                   
REMARK 500    GLU A 413     -158.94    -80.47                                   
REMARK 500    ASN A 414       18.72     57.37                                   
REMARK 500    HIS A 472       26.53   -150.92                                   
REMARK 500    ASP A 474       48.68    -82.47                                   
REMARK 500    ARG A 475        9.12   -160.13                                   
REMARK 500    SER A 476      162.48     65.07                                   
REMARK 500    LYS A 491      -81.62     51.36                                   
REMARK 500    SER A 508       47.86    -74.49                                   
REMARK 500    ASN A 509       83.68     51.49                                   
REMARK 500    PRO A 519     -167.65    -75.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FPJ A 601                 
DBREF  6CZ5 A  132   607  UNP    O00571   DDX3X_HUMAN    132    607             
SEQADV 6CZ5 GLY A  128  UNP  O00571              EXPRESSION TAG                 
SEQADV 6CZ5 SER A  129  UNP  O00571              EXPRESSION TAG                 
SEQADV 6CZ5 PHE A  130  UNP  O00571              EXPRESSION TAG                 
SEQADV 6CZ5 THR A  131  UNP  O00571              EXPRESSION TAG                 
SEQADV 6CZ5 CYS A  228  UNP  O00571    SER   228 ENGINEERED MUTATION            
SEQRES   1 A  480  GLY SER PHE THR ASP GLU ASP ASP TRP SER LYS PRO LEU          
SEQRES   2 A  480  PRO PRO SER GLU ARG LEU GLU GLN GLU LEU PHE SER GLY          
SEQRES   3 A  480  GLY ASN THR GLY ILE ASN PHE GLU LYS TYR ASP ASP ILE          
SEQRES   4 A  480  PRO VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS ILE          
SEQRES   5 A  480  GLU SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE MET          
SEQRES   6 A  480  GLY ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR PRO          
SEQRES   7 A  480  VAL GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS ARG          
SEQRES   8 A  480  ASP LEU MET ALA CYS ALA GLN THR GLY CYS GLY LYS THR          
SEQRES   9 A  480  ALA ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR SER          
SEQRES  10 A  480  ASP GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU ASN          
SEQRES  11 A  480  GLY ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER LEU          
SEQRES  12 A  480  VAL LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE TYR          
SEQRES  13 A  480  GLU GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL ARG          
SEQRES  14 A  480  PRO CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN GLN          
SEQRES  15 A  480  ILE ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL ALA          
SEQRES  16 A  480  THR PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY LYS          
SEQRES  17 A  480  ILE GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP GLU          
SEQRES  18 A  480  ALA ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN ILE          
SEQRES  19 A  480  ARG ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS GLY          
SEQRES  20 A  480  VAL ARG HIS THR MET MET PHE SER ALA THR PHE PRO LYS          
SEQRES  21 A  480  GLU ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU TYR          
SEQRES  22 A  480  ILE PHE LEU ALA VAL GLY ARG VAL GLY SER THR SER GLU          
SEQRES  23 A  480  ASN ILE THR GLN LYS VAL VAL TRP VAL GLU GLU SER ASP          
SEQRES  24 A  480  LYS ARG SER PHE LEU LEU ASP LEU LEU ASN ALA THR GLY          
SEQRES  25 A  480  LYS ASP SER LEU THR LEU VAL PHE VAL GLU THR LYS LYS          
SEQRES  26 A  480  GLY ALA ASP SER LEU GLU ASP PHE LEU TYR HIS GLU GLY          
SEQRES  27 A  480  TYR ALA CYS THR SER ILE HIS GLY ASP ARG SER GLN ARG          
SEQRES  28 A  480  ASP ARG GLU GLU ALA LEU HIS GLN PHE ARG SER GLY LYS          
SEQRES  29 A  480  SER PRO ILE LEU VAL ALA THR ALA VAL ALA ALA ARG GLY          
SEQRES  30 A  480  LEU ASP ILE SER ASN VAL LYS HIS VAL ILE ASN PHE ASP          
SEQRES  31 A  480  LEU PRO SER ASP ILE GLU GLU TYR VAL HIS ARG ILE GLY          
SEQRES  32 A  480  ARG THR GLY ARG VAL GLY ASN LEU GLY LEU ALA THR SER          
SEQRES  33 A  480  PHE PHE ASN GLU ARG ASN ILE ASN ILE THR LYS ASP LEU          
SEQRES  34 A  480  LEU ASP LEU LEU VAL GLU ALA LYS GLN GLU VAL PRO SER          
SEQRES  35 A  480  TRP LEU GLU ASN MET ALA TYR GLU HIS HIS TYR LYS GLY          
SEQRES  36 A  480  SER SER ARG GLY ARG SER LYS SER SER ARG PHE SER GLY          
SEQRES  37 A  480  GLY PHE GLY ALA ARG ASP TYR ARG GLN SER SER GLY              
HET    FPJ  A 601      27                                                       
HETNAM     FPJ 5'-O-[(R)-HYDROXY(PROPANOYLAMINO)PHOSPHORYL]ADENOSINE            
FORMUL   2  FPJ    C13 H19 N6 O7 P                                              
HELIX    1 AA1 SER A  143  PHE A  151  1                                   9    
HELIX    2 AA2 GLY A  188  THR A  198  1                                  11    
HELIX    3 AA3 THR A  204  GLU A  216  1                                  13    
HELIX    4 AA4 THR A  231  GLY A  246  1                                  16    
HELIX    5 AA5 GLY A  248  ALA A  253  1                                   6    
HELIX    6 AA6 THR A  275  TYR A  291  1                                  17    
HELIX    7 AA7 ASP A  305  ARG A  315  1                                  11    
HELIX    8 AA8 THR A  323  ARG A  333  1                                  11    
HELIX    9 AA9 GLU A  348  MET A  355  1                                   8    
HELIX   10 AB1 PHE A  357  GLU A  366  1                                  10    
HELIX   11 AB2 PRO A  386  LEU A  397  1                                  12    
HELIX   12 AB3 GLU A  423  SER A  425  5                                   3    
HELIX   13 AB4 ASP A  426  ALA A  437  1                                  12    
HELIX   14 AB5 THR A  450  HIS A  463  1                                  14    
HELIX   15 AB6 ARG A  475  SER A  489  1                                  15    
HELIX   16 AB7 ASP A  521  GLY A  530  1                                  10    
HELIX   17 AB8 ASN A  546  ASN A  551  5                                   6    
HELIX   18 AB9 ILE A  552  ALA A  563  1                                  12    
HELIX   19 AC1 PRO A  568  ASN A  573  1                                   6    
SHEET    1 AA1 7 PRO A 297  VAL A 300  0                                        
SHEET    2 AA1 7 LEU A 319  ALA A 322  1  O  VAL A 321   N  CYS A 298           
SHEET    3 AA1 7 SER A 269  LEU A 272  1  N  VAL A 271   O  LEU A 320           
SHEET    4 AA1 7 TYR A 343  LEU A 346  1  O  VAL A 345   N  LEU A 272           
SHEET    5 AA1 7 HIS A 377  SER A 382  1  O  HIS A 377   N  LEU A 344           
SHEET    6 AA1 7 LEU A 220  CYS A 223  1  N  ALA A 222   O  MET A 380           
SHEET    7 AA1 7 ILE A 401  ALA A 404  1  O  ILE A 401   N  MET A 221           
SHEET    1 AA2 6 ILE A 415  TRP A 421  0                                        
SHEET    2 AA2 6 GLY A 539  PHE A 545  1  O  GLY A 539   N  THR A 416           
SHEET    3 AA2 6 HIS A 512  ASN A 515  1  N  VAL A 513   O  LEU A 540           
SHEET    4 AA2 6 THR A 444  VAL A 448  1  N  LEU A 445   O  ILE A 514           
SHEET    5 AA2 6 ILE A 494  THR A 498  1  O  LEU A 495   N  THR A 444           
SHEET    6 AA2 6 CYS A 468  ILE A 471  1  N  THR A 469   O  ILE A 494           
LINK         SG  CYS A 228                 C13 FPJ A 601     1555   1555  1.80  
SITE     1 AC1  7 TYR A 200  ARG A 202  THR A 204  GLN A 207                    
SITE     2 AC1  7 CYS A 228  GLY A 229  GLU A 285                               
CRYST1   53.960  101.090  105.690  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018532  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009892  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009462        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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