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Database: PDB
Entry: 4QFG
LinkDB: 4QFG
Original site: 4QFG 
HEADER    SIGNALING PROTEIN/INHIBITOR             20-MAY-14   4QFG              
TITLE     STRUCTURE OF AMPK IN COMPLEX WITH STAUROSPORINE INHIBITOR AND IN THE  
TITLE    2 ABSENCE OF A SYNTHETIC ACTIVATOR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: AMPK ALPHA1;                                               
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1, ACETYL-COA CARBOXYLASE KINASE, ACACA  
COMPND   6 KINASE, HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE, HMGCR KINASE,    
COMPND   7 TAU-PROTEIN KINASE PRKAA1;                                           
COMPND   8 EC: 2.7.11.1, 2.7.11.27, 2.7.11.31, 2.7.11.26;                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: AMPK BETA1;                                                
COMPND  15 SYNONYM: AMPK SUBUNIT BETA-1, AMPKB, 5'-AMP-ACTIVATED PROTEIN KINASE 
COMPND  16 40 KDA SUBUNIT;                                                      
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MUTATION: YES;                                                       
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  21 CHAIN: C;                                                            
COMPND  22 FRAGMENT: AMPK GAMMA1;                                               
COMPND  23 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: AMPK1, PRKAA1, PRKAA1 AMPK1;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 GENE: PRKAB1;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  17 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE  18 ORGANISM_TAXID: 10116;                                               
SOURCE  19 GENE: PRKAG1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CBM, KINASE, AMPK, SIGNALING PROTEIN-INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.CALABRESE,R.G.KURUMBAIL                                           
REVDAT   5   22-NOV-17 4QFG    1       REMARK                                   
REVDAT   4   16-AUG-17 4QFG    1       SOURCE REMARK                            
REVDAT   3   20-AUG-14 4QFG    1       JRNL                                     
REVDAT   2   13-AUG-14 4QFG    1       JRNL                                     
REVDAT   1   06-AUG-14 4QFG    0                                                
JRNL        AUTH   M.F.CALABRESE,F.RAJAMOHAN,M.S.HARRIS,N.L.CASPERS,R.MAGYAR,   
JRNL        AUTH 2 J.M.WITHKA,H.WANG,K.A.BORZILLERI,P.V.SAHASRABUDHE,L.R.HOTH,  
JRNL        AUTH 3 K.F.GEOGHEGAN,S.HAN,J.BROWN,T.A.SUBASHI,A.R.REYES,           
JRNL        AUTH 4 R.K.FRISBIE,J.WARD,R.A.MILLER,J.A.LANDRO,A.T.LONDREGAN,      
JRNL        AUTH 5 P.A.CARPINO,S.CABRAL,A.C.SMITH,E.L.CONN,K.O.CAMERON,X.QIU,   
JRNL        AUTH 6 R.G.KURUMBAIL                                                
JRNL        TITL   STRUCTURAL BASIS FOR AMPK ACTIVATION: NATURAL AND SYNTHETIC  
JRNL        TITL 2 LIGANDS REGULATE KINASE ACTIVITY FROM OPPOSITE POLES BY      
JRNL        TITL 3 DIFFERENT MOLECULAR MECHANISMS.                              
JRNL        REF    STRUCTURE                     V.  22  1161 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25066137                                                     
JRNL        DOI    10.1016/J.STR.2014.06.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.5                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24332                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
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   (%)  : 4.960                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1208                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.46                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.61                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.98                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2894                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2404                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2773                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2399                   
REMARK   3   BIN FREE R VALUE                        : 0.2519                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.18                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 121                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6491                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 91.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.59900                                             
REMARK   3    B22 (A**2) : -7.59900                                             
REMARK   3    B33 (A**2) : 15.19790                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.791               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.886                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.836                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6743   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9180   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2309   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 136    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 969    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6743   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 880    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7739   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.24                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   31.1704  -75.0579  -16.3724           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0292 T22:   -0.1426                                    
REMARK   3     T33:   -0.2722 T12:    0.0493                                    
REMARK   3     T13:   -0.0504 T23:   -0.1175                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1138 L22:    1.3904                                    
REMARK   3     L33:    2.1489 L12:   -0.1033                                    
REMARK   3     L13:   -0.1192 L23:    0.5198                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0024 S12:    0.0751 S13:    0.0876                     
REMARK   3     S21:   -0.2579 S22:   -0.0745 S23:    0.1198                     
REMARK   3     S31:   -0.4840 S32:   -0.3884 S33:    0.0721                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   37.3148  -68.0219  -31.2415           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2121 T22:   -0.0047                                    
REMARK   3     T33:   -0.0536 T12:    0.1247                                    
REMARK   3     T13:    0.0316 T23:   -0.0736                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5831 L22:    0.3836                                    
REMARK   3     L33:    4.3420 L12:   -0.7990                                    
REMARK   3     L13:   -2.0189 L23:    1.6617                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0697 S12:   -0.0064 S13:    0.1023                     
REMARK   3     S21:   -0.1323 S22:    0.0516 S23:    0.1068                     
REMARK   3     S31:   -0.4078 S32:   -0.0735 S33:    0.0182                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   25.7772  -40.1826   16.7858           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3503 T22:    0.3360                                    
REMARK   3     T33:    0.2905 T12:    0.0869                                    
REMARK   3     T13:    0.0686 T23:   -0.1718                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6855 L22:    2.1777                                    
REMARK   3     L33:    2.2410 L12:   -1.4227                                    
REMARK   3     L13:    0.2618 L23:    0.4266                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0380 S12:   -0.1099 S13:    0.2107                     
REMARK   3     S21:   -0.2971 S22:    0.0911 S23:   -0.2056                     
REMARK   3     S31:   -0.6039 S32:    0.2414 S33:   -0.0531                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085987.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24332                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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   (%): 67.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 750 MM AMMONIUM SULFATE, 500 MM          
REMARK 280  LITHIUM SULFATE, 100 MM TRI-SODIUM CITRATE, 1% ETHYLENE GLYCOL,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      134.68667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      269.37333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      202.03000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      336.71667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.34333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      134.68667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      269.37333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      336.71667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      202.03000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       67.34333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: BIOLOGICAL UNIT IS COMPRISED OF A HETEROTRIMER OF THE ALPHA, 
REMARK 300 BETA, AND GAMMA SUBUNITS (CHAINS A, B, C)                            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -273.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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   BIOMT1   2  0.500000 -0.866025  0.000000      -62.18500            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000     -107.70758            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -67.34333            
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    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLU A   279                                                      
REMARK 465     ASP A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     TYR A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     MET A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     ASP A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     GLU A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     GLU A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     CYS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PHE A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     CYS A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     CYS A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     TYR A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     ASP A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     VAL A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     TYR A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     ILE A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     ASN A   330                                                      
REMARK 465     ARG A   331                                                      
REMARK 465     ARG A   332                                                      
REMARK 465     ILE A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     ALA A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     PHE A   340                                                      
REMARK 465     TYR A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     ALA A   343                                                      
REMARK 465     THR A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     PRO A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     ASP A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     LEU A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     ARG A   358                                                      
REMARK 465     PRO A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     ARG A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     PHE A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     VAL A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     THR A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     ARG A   373                                                      
REMARK 465     ALA A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     LEU A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     LEU A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     LYS A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     GLY A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     GLY A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     ALA A   525                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     MET B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     LYS B   172                                                      
REMARK 465     CYS B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     PRO B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     TYR B   187                                                      
REMARK 465     HIS B   188                                                      
REMARK 465     GLN B   189                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     PRO B   191                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     ILE B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     PRO B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     GLY B   220                                                      
REMARK 465     ILE B   221                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ASN C    24                                                      
REMARK 465     ASP C   123                                                      
REMARK 465     SER C   124                                                      
REMARK 465     PHE C   125                                                      
REMARK 465     LYS C   126                                                      
REMARK 465     SER C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     TYR C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     GLU C   273                                                      
REMARK 465     GLY C   274                                                      
REMARK 465     VAL C   275                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     THR C   324                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     PRO C   330                                                      
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     ARG A 527    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     SER B 222    CB   OG                                             
REMARK 470     CYS B 223    CB   SG                                             
REMARK 470     ASP B 224    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     ASP B 246    CG   OD1  OD2                                       
REMARK 470     LYS C  99    CG   CD   CE   NZ                                   
REMARK 470     GLN C 104    CG   CD   OE1  NE2                                  
REMARK 470     TYR C 106    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 169    CG   CD   CE   NZ                                   
REMARK 470     ASP C 231    CG   OD1  OD2                                       
REMARK 470     GLU C 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 233    CG   CD   CE   NZ                                   
REMARK 470     ARG C 235    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 302    CG1  CG2                                            
REMARK 470     ASP C 303    CG   OD1  OD2                                       
REMARK 470     GLU C 304    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 305    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP C 306    CG   OD1  OD2                                       
REMARK 470     VAL C 307    CG1  CG2                                            
REMARK 470     VAL C 308    CG1  CG2                                            
REMARK 470     LYS C 309    CG   CD   CE   NZ                                   
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    PHE A  27      -73.30   -111.64                                   
REMARK 500    LEU A  55     -154.37    -94.56                                   
REMARK 500    ARG A  72       83.28   -164.77                                   
REMARK 500    ASP A 139       45.17     81.14                                   
REMARK 500    MET A 151       76.42     34.56                                   
REMARK 500    TPO A 172       97.02    -19.42                                   
REMARK 500    ASP A 421        8.76     59.77                                   
REMARK 500    VAL A 427      -87.11    -85.28                                   
REMARK 500    VAL A 440      -64.47   -102.11                                   
REMARK 500    VAL A 454      -75.00    -87.18                                   
REMARK 500    SER A 530      133.54    -38.58                                   
REMARK 500    THR B  85       21.38    -77.34                                   
REMARK 500    ASP B 108      -91.77    -70.83                                   
REMARK 500    GLN B 109      -55.64   -138.49                                   
REMARK 500    CYS B 223     -156.10    -70.81                                   
REMARK 500    HIS B 233      -35.23    -35.99                                   
REMARK 500    ASN B 237       -4.29     76.91                                   
REMARK 500    LYS B 245     -110.46    -96.98                                   
REMARK 500    ASP B 246       33.90    -79.01                                   
REMARK 500    LYS B 258     -129.55     56.11                                   
REMARK 500    ILE C 105       92.06    -65.50                                   
REMARK 500    LEU C 121       71.37     43.55                                   
REMARK 500    ASP C 238     -157.18   -145.48                                   
REMARK 500    ILE C 239      119.23   -163.02                                   
REMARK 500    ASP C 303     -108.58    -77.85                                   
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 STU A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QFS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QFT   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ENGINEERED INSERTION ASGGPGGS                                        
DBREF  4QFG A    0   469  UNP    P54645   AAPK1_RAT       11    480             
DBREF  4QFG A  525   548  UNP    P54645   AAPK1_RAT      536    559             
DBREF  4QFG B   68   270  UNP    P80386   AAKB1_RAT       67    269             
DBREF  4QFG C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4QFG GLY A   -1  UNP  P54645              EXPRESSION TAG                 
SEQADV 4QFG ALA A  517  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG SER A  518  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG GLY A  519  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG GLY A  520  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG PRO A  521  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG GLY A  522  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG GLY A  523  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG SER A  524  UNP  P54645              SEE REMARK 999                 
SEQADV 4QFG MET B   67  UNP  P80386              EXPRESSION TAG                 
SEQADV 4QFG ASP B  108  UNP  P80386    SER   107 ENGINEERED MUTATION            
SEQRES   1 A  503  GLY ALA THR ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL          
SEQRES   2 A  503  LYS ILE GLY HIS TYR ILE LEU GLY ASP THR LEU GLY VAL          
SEQRES   3 A  503  GLY THR PHE GLY LYS VAL LYS VAL GLY LYS HIS GLU LEU          
SEQRES   4 A  503  THR GLY HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN          
SEQRES   5 A  503  LYS ILE ARG SER LEU ASP VAL VAL GLY LYS ILE ARG ARG          
SEQRES   6 A  503  GLU ILE GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE          
SEQRES   7 A  503  ILE LYS LEU TYR GLN VAL ILE SER THR PRO SER ASP ILE          
SEQRES   8 A  503  PHE MET VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  503  ASP TYR ILE CYS LYS ASN GLY ARG LEU ASP GLU LYS GLU          
SEQRES  10 A  503  SER ARG ARG LEU PHE GLN GLN ILE LEU SER GLY VAL ASP          
SEQRES  11 A  503  TYR CYS HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS          
SEQRES  12 A  503  PRO GLU ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS          
SEQRES  13 A  503  ILE ALA ASP PHE GLY LEU SER ASN MET MET SER ASP GLY          
SEQRES  14 A  503  GLU PHE LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA          
SEQRES  15 A  503  ALA PRO GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO          
SEQRES  16 A  503  GLU VAL ASP ILE TRP SER SER GLY VAL ILE LEU TYR ALA          
SEQRES  17 A  503  LEU LEU CYS GLY THR LEU PRO PHE ASP ASP ASP HIS VAL          
SEQRES  18 A  503  PRO THR LEU PHE LYS LYS ILE CYS ASP GLY ILE PHE TYR          
SEQRES  19 A  503  THR PRO GLN TYR LEU ASN PRO SER VAL ILE SER LEU LEU          
SEQRES  20 A  503  LYS HIS MET LEU GLN VAL ASP PRO MET LYS ARG ALA THR          
SEQRES  21 A  503  ILE LYS ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN ASP          
SEQRES  22 A  503  LEU PRO LYS TYR LEU PHE PRO GLU ASP PRO SER TYR SER          
SEQRES  23 A  503  SER THR MET ILE ASP ASP GLU ALA LEU LYS GLU VAL CYS          
SEQRES  24 A  503  GLU LYS PHE GLU CYS SER GLU GLU GLU VAL LEU SER CYS          
SEQRES  25 A  503  LEU TYR ASN ARG ASN HIS GLN ASP PRO LEU ALA VAL ALA          
SEQRES  26 A  503  TYR HIS LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLU          
SEQRES  27 A  503  ALA LYS ASP PHE TYR LEU ALA THR SER PRO PRO ASP SER          
SEQRES  28 A  503  PHE LEU ASP ASP HIS HIS LEU THR ARG PRO HIS PRO GLU          
SEQRES  29 A  503  ARG VAL PRO PHE LEU VAL ALA GLU THR PRO ARG ALA ARG          
SEQRES  30 A  503  HIS THR LEU ASP GLU LEU ASN PRO GLN LYS SER LYS HIS          
SEQRES  31 A  503  GLN GLY VAL ARG LYS ALA LYS TRP HIS LEU GLY ILE ARG          
SEQRES  32 A  503  SER GLN SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS          
SEQRES  33 A  503  ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL          
SEQRES  34 A  503  ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL          
SEQRES  35 A  503  THR SER THR PHE SER LYS MET SER LEU GLN LEU TYR GLN          
SEQRES  36 A  503  VAL ASP SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE          
SEQRES  37 A  503  ASP ASP GLU ALA SER GLY GLY PRO GLY GLY SER ALA PRO          
SEQRES  38 A  503  ARG PRO GLY SER HIS THR ILE GLU PHE PHE GLU MET CYS          
SEQRES  39 A  503  ALA ASN LEU ILE LYS ILE LEU ALA GLN                          
SEQRES   1 B  204  MET GLU VAL ASN GLU LYS ALA PRO ALA GLN ALA ARG PRO          
SEQRES   2 B  204  THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL TYR          
SEQRES   3 B  204  LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO LEU          
SEQRES   4 B  204  THR ARG ASP GLN ASN ASN PHE VAL ALA ILE LEU ASP LEU          
SEQRES   5 B  204  PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP GLY          
SEQRES   6 B  204  GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR SER          
SEQRES   7 B  204  GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS LYS          
SEQRES   8 B  204  THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP SER          
SEQRES   9 B  204  GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER PRO          
SEQRES  10 B  204  PRO GLY PRO TYR HIS GLN GLU PRO TYR ILE SER LYS PRO          
SEQRES  11 B  204  GLU GLU ARG PHE LYS ALA PRO PRO ILE LEU PRO PRO HIS          
SEQRES  12 B  204  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER          
SEQRES  13 B  204  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES  14 B  204  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL          
SEQRES  15 B  204  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES  16 B  204  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 C  330  MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU          
SEQRES   2 C  330  ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER          
SEQRES   3 C  330  VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP          
SEQRES   4 C  330  LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR          
SEQRES   5 C  330  SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR          
SEQRES   6 C  330  ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS          
SEQRES   7 C  330  GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE          
SEQRES   8 C  330  ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN          
SEQRES   9 C  330  ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG          
SEQRES  10 C  330  GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS          
SEQRES  11 C  330  ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER          
SEQRES  12 C  330  LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP          
SEQRES  13 C  330  PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS          
SEQRES  14 C  330  ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE          
SEQRES  15 C  330  PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU          
SEQRES  16 C  330  GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR          
SEQRES  17 C  330  THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN          
SEQRES  18 C  330  HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY          
SEQRES  19 C  330  ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN          
SEQRES  20 C  330  LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER          
SEQRES  21 C  330  VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU          
SEQRES  22 C  330  GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA          
SEQRES  23 C  330  ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU          
SEQRES  24 C  330  VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL          
SEQRES  25 C  330  SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY          
SEQRES  26 C  330  GLY GLU LYS LYS PRO                                          
MODRES 4QFG TPO A  172  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 172      11                                                       
HET    STU  A 601      61                                                       
HET     CL  A 602       1                                                       
HET     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET    SO4  A 605       5                                                       
HET    AMP  C 401      23                                                       
HET    SO4  C 402       5                                                       
HET    SO4  C 403       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     STU STAUROSPORINE                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   8  SO4    3(O4 S 2-)                                                   
FORMUL   9  AMP    C10 H14 N5 O7 P                                              
HELIX    1   1 ARG A   49  ARG A   53  1                                   5    
HELIX    2   2 VAL A   57  PHE A   71  1                                  15    
HELIX    3   3 LEU A  101  ASN A  108  1                                   8    
HELIX    4   4 ASP A  112  ARG A  132  1                                  21    
HELIX    5   5 ALA A  181  SER A  186  1                                   6    
HELIX    6   6 GLY A  192  GLY A  210  1                                  19    
HELIX    7   7 HIS A  218  GLY A  229  1                                  12    
HELIX    8   8 ASN A  238  LEU A  249  1                                  12    
HELIX    9   9 ASP A  252  ARG A  256  5                                   5    
HELIX   10  10 THR A  258  GLU A  264  1                                   7    
HELIX   11  11 HIS A  265  GLN A  270  1                                   6    
HELIX   12  12 ARG A  405  LEU A  420  1                                  16    
HELIX   13  13 SER A  530  LYS A  544  1                                  15    
HELIX   14  14 PHE B   97  ASN B   99  5                                   3    
HELIX   15  15 PHE B  163  GLN B  171  1                                   9    
HELIX   16  16 PRO B  207  LEU B  211  5                                   5    
HELIX   17  17 ASN B  232  LEU B  236  5                                   5    
HELIX   18  18 SER C   26  HIS C   35  1                                  10    
HELIX   19  19 ARG C   36  ILE C   41  5                                   6    
HELIX   20  20 GLN C   55  GLY C   67  1                                  13    
HELIX   21  21 ILE C   87  TYR C   97  1                                  11    
HELIX   22  22 ILE C  105  HIS C  111  1                                   7    
HELIX   23  23 LYS C  112  TYR C  120  1                                   9    
HELIX   24  24 SER C  136  ASN C  147  1                                  12    
HELIX   25  25 HIS C  168  PHE C  182  1                                  15    
HELIX   26  26 PRO C  185  LYS C  190  1                                   6    
HELIX   27  27 SER C  191  GLN C  196  1                                   6    
HELIX   28  28 PRO C  211  ARG C  223  1                                  13    
HELIX   29  29 LYS C  242  GLU C  251  1                                  10    
HELIX   30  30 SER C  260  LEU C  265  1                                   6    
HELIX   31  31 GLN C  266  ARG C  268  5                                   3    
HELIX   32  32 THR C  283  GLU C  295  1                                  13    
HELIX   33  33 LEU C  314  ALA C  320  1                                   7    
SHEET    1   A 6 LYS A  12  ILE A  13  0                                        
SHEET    2   A 6 TYR A  16  GLY A  23 -1  O  TYR A  16   N  ILE A  13           
SHEET    3   A 6 LYS A  29  HIS A  35 -1  O  VAL A  32   N  GLY A  19           
SHEET    4   A 6 LYS A  41  ASN A  48 -1  O  VAL A  44   N  LYS A  31           
SHEET    5   A 6 ASP A  88  GLU A  94 -1  O  ILE A  89   N  LEU A  47           
SHEET    6   A 6 LEU A  79  SER A  84 -1  N  ILE A  83   O  PHE A  90           
SHEET    1   B 3 GLY A  99  GLU A 100  0                                        
SHEET    2   B 3 VAL A 145  LEU A 147 -1  O  LEU A 147   N  GLY A  99           
SHEET    3   B 3 ALA A 153  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1   C 2 VAL A 135  HIS A 137  0                                        
SHEET    2   C 2 SER A 161  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1   D 7 HIS A 397  LEU A 398  0                                        
SHEET    2   D 7 TYR B 240  LEU B 242 -1  O  ALA B 241   N  HIS A 397           
SHEET    3   D 7 VAL B 248  TYR B 257 -1  O  VAL B 250   N  LEU B 242           
SHEET    4   D 7 LYS B 260  PRO B 269 -1  O  VAL B 262   N  HIS B 255           
SHEET    5   D 7 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 265           
SHEET    6   D 7 ALA C  70  ASP C  75  1  O  TRP C  74   N  PHE C  50           
SHEET    7   D 7 SER C  80  THR C  86 -1  O  LEU C  85   N  ALA C  71           
SHEET    1   E 5 ILE A 400  SER A 402  0                                        
SHEET    2   E 5 TYR A 459  ILE A 466 -1  O  LEU A 461   N  ILE A 400           
SHEET    3   E 5 PHE A 444  TYR A 452 -1  N  TYR A 452   O  LEU A 460           
SHEET    4   E 5 TYR A 431  LYS A 437 -1  N  LEU A 432   O  LEU A 449           
SHEET    5   E 5 GLU A 423  VAL A 426 -1  N  LYS A 425   O  ARG A 433           
SHEET    1   F 3 PRO B  79  TRP B  84  0                                        
SHEET    2   F 3 PHE B 112  ASP B 117 -1  O  ALA B 114   N  PHE B  82           
SHEET    3   F 3 THR B 106  ARG B 107 -1  N  THR B 106   O  VAL B 113           
SHEET    1   G 4 LEU B 103  PRO B 104  0                                        
SHEET    2   G 4 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3   G 4 GLY B 121  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4   G 4 TRP B 133  THR B 134 -1  O  THR B 134   N  PHE B 127           
SHEET    1   H 5 LEU B 103  PRO B 104  0                                        
SHEET    2   H 5 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3   H 5 GLY B 121  VAL B 129 -1  O  PHE B 128   N  TYR B  92           
SHEET    4   H 5 VAL B 149  VAL B 155 -1  O  VAL B 155   N  GLY B 121           
SHEET    5   H 5 ILE B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1   I 2 ARG C 151  ILE C 155  0                                        
SHEET    2   I 2 THR C 162  THR C 167 -1  O  TYR C 164   N  VAL C 154           
SHEET    1   J 3 VAL C 206  ARG C 207  0                                        
SHEET    2   J 3 ALA C 226  VAL C 230  1  O  PRO C 228   N  VAL C 206           
SHEET    3   J 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1   K 3 LYS C 277  TYR C 279  0                                        
SHEET    2   K 3 ARG C 298  VAL C 302  1  O  VAL C 302   N  CYS C 278           
SHEET    3   K 3 VAL C 308  SER C 313 -1  O  GLY C 310   N  VAL C 301           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.36  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.33  
SITE     1 AC1 16 LEU A  22  GLY A  23  GLY A  25  VAL A  30                    
SITE     2 AC1 16 ALA A  43  ILE A  77  GLU A  94  TYR A  95                    
SITE     3 AC1 16 VAL A  96  GLY A  99  GLU A 100  GLU A 143                    
SITE     4 AC1 16 ASN A 144  LEU A 146  ALA A 156  ASP A 157                    
SITE     1 AC2  1 VAL A  24                                                     
SITE     1 AC3  2 LYS A  34  LYS A  41                                          
SITE     1 AC4  2 SER A  97  ALA A 149                                          
SITE     1 AC5  5 LYS A  29  ASN A  48  LYS A  51  ARG B  83                    
SITE     2 AC5  5 ASN B 110                                                     
SITE     1 AC6 12 HIS C 150  THR C 199  ILE C 203  ALA C 204                    
SITE     2 AC6 12 VAL C 224  SER C 225  ALA C 226  ARG C 298                    
SITE     3 AC6 12 ILE C 311  SER C 313  SER C 315  ASP C 316                    
SITE     1 AC7  5 THR C  86  ILE C  87  THR C  88  HIS C 150                    
SITE     2 AC7  5 ARG C 151                                                     
SITE     1 AC8  4 SER C 241  PHE C 243  HIS C 297  ARG C 298                    
CRYST1  124.370  124.370  404.060  90.00  90.00 120.00 P 61 2 2     12          
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      0.008041  0.004642  0.000000        0.00000                         
SCALE2      0.000000  0.009284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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