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Database: PDB
Entry: 4DFY
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Original site: 4DFY 
HEADER    TRANSFERASE                             24-JAN-12   4DFY              
TITLE     CRYSTAL STRUCTURE OF R194A MUTANT OF CAMP-DEPENDENT PROTEIN KINASE    
TITLE    2 WITH UNPHOSPHORYLATED ACTIVATION LOOP                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN KINASE FOLD, SERINE/THREONINE KINASE ACTIVITY, CAMP-DEPENDENT 
KEYWDS   2 PROTEIN KINASE REGULATORY SUBUNIT, PKI, PHOSPHORYLATION, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.STEICHEN,M.KUCHINSKAS,J.YANG,S.S.TAYLOR                           
REVDAT   3   16-MAY-12 4DFY    1       JRNL                                     
REVDAT   2   29-FEB-12 4DFY    1       JRNL                                     
REVDAT   1   15-FEB-12 4DFY    0                                                
JRNL        AUTH   J.M.STEICHEN,M.KUCHINSKAS,M.M.KESHWANI,J.YANG,J.A.ADAMS,     
JRNL        AUTH 2 S.S.TAYLOR                                                   
JRNL        TITL   STRUCTURAL BASIS FOR THE REGULATION OF PROTEIN KINASE A BY   
JRNL        TITL 2 ACTIVATION LOOP PHOSPHORYLATION.                             
JRNL        REF    J.BIOL.CHEM.                  V. 287 14672 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22334660                                                     
JRNL        DOI    10.1074/JBC.M111.335091                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 16987                          
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) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.252                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 915                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 699                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 40                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4984                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 104.57                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : 0.05000                                              
REMARK   3    B33 (A**2) : -0.08000                                             
REMARK   3    B12 (A**2) : 0.03000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.484         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.471         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 61.726        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5103 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6912 ; 1.328 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   618 ; 5.590 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   241 ;39.075 ;24.315       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   861 ;19.104 ;15.035       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;18.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   755 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3870 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3107 ; 0.586 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4979 ; 1.143 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1996 ; 1.377 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1933 ; 2.462 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     14       A     350      1                      
REMARK   3           1     E     14       E     350      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2455 ; 0.070 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2455 ; 0.610 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    14        A   126                          
REMARK   3    RESIDUE RANGE :   A   333        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A): -60.3050  13.2430  -1.0690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2838 T22:   0.5401                                     
REMARK   3      T33:   0.3564 T12:  -0.0813                                     
REMARK   3      T13:  -0.0912 T23:   0.1512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6127 L22:   2.4541                                     
REMARK   3      L33:   6.1906 L12:  -1.4201                                     
REMARK   3      L13:  -0.8186 L23:   2.1914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1821 S12:   0.1299 S13:   0.1439                       
REMARK   3      S21:  -0.0760 S22:   0.0172 S23:   0.1916                       
REMARK   3      S31:  -0.3112 S32:  -1.2832 S33:   0.1649                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   127        A   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -61.3700  21.8770  26.3060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2811 T22:   0.3622                                     
REMARK   3      T33:   0.4042 T12:   0.2610                                     
REMARK   3      T13:   0.0913 T23:   0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6291 L22:   2.0404                                     
REMARK   3      L33:   7.9667 L12:   1.0565                                     
REMARK   3      L13:   1.0256 L23:  -0.2955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0364 S12:   0.0313 S13:  -0.0434                       
REMARK   3      S21:   0.0591 S22:  -0.0380 S23:  -0.0463                       
REMARK   3      S31:  -0.0885 S32:  -0.4255 S33:   0.0744                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    14        E   126                          
REMARK   3    RESIDUE RANGE :   E   333        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1230  30.0980  20.2510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5210 T22:   0.2933                                     
REMARK   3      T33:   0.2791 T12:  -0.3026                                     
REMARK   3      T13:  -0.0322 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2206 L22:   3.5120                                     
REMARK   3      L33:   2.4058 L12:  -0.5007                                     
REMARK   3      L13:   0.2921 L23:  -0.2957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0320 S12:  -0.2420 S13:  -0.1088                       
REMARK   3      S21:   0.4712 S22:   0.1044 S23:   0.0372                       
REMARK   3      S31:  -0.7979 S32:   0.3179 S33:  -0.0723                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   127        E   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8970   4.3770   7.8980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1374 T22:   0.3322                                     
REMARK   3      T33:   0.2947 T12:  -0.0879                                     
REMARK   3      T13:  -0.0169 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5068 L22:   5.9456                                     
REMARK   3      L33:   3.4786 L12:   1.7040                                     
REMARK   3      L13:   1.4790 L23:   1.6828                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0881 S12:   0.0465 S13:  -0.0418                       
REMARK   3      S21:   0.4488 S22:   0.3722 S23:  -0.0981                       
REMARK   3      S31:   0.1398 S32:   0.4708 S33:  -0.2841                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4DFY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070279.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL (SI 111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.997                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.1000                            
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) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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 1RDQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, 800 MM SODIUM FORMATE,      
REMARK 280  10% PEG 8000, 10% PEG 1000, PH 7.5, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 277.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      115.97267            
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       57.98633            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       57.98633            
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      115.97267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       57.98633            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     LYS A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     VAL A   191                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     GLY A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     THR A   195                                                      
REMARK 465     TRP A   196                                                      
REMARK 465     THR A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     CYS A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ASN A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     TYR A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     MET E   -20                                                      
REMARK 465     GLY E   -19                                                      
REMARK 465     SER E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     LEU E    -7                                                      
REMARK 465     VAL E    -6                                                      
REMARK 465     PRO E    -5                                                      
REMARK 465     ARG E    -4                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     LYS E   189                                                      
REMARK 465     ARG E   190                                                      
REMARK 465     VAL E   191                                                      
REMARK 465     LYS E   192                                                      
REMARK 465     GLY E   193                                                      
REMARK 465     ALA E   194                                                      
REMARK 465     THR E   195                                                      
REMARK 465     TRP E   196                                                      
REMARK 465     THR E   197                                                      
REMARK 465     LEU E   198                                                      
REMARK 465     LYS E   319                                                      
REMARK 465     GLY E   320                                                      
REMARK 465     PRO E   321                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     THR E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     ASN E   326                                                      
REMARK 465     PHE E   327                                                      
REMARK 465     ASP E   328                                                      
REMARK 465     ASP E   329                                                      
REMARK 465     TYR E   330                                                      
REMARK 465     GLU E   331                                                      
REMARK 465     GLU E   332                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     LYS A  83    CE   NZ                                             
REMARK 470     GLU A  91    CD   OE1  OE2                                       
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     HIS A 131    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 142    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 168    CG   CD   CE   NZ                                   
REMARK 470     GLN A 176    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 185    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 187    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 295    CG   CD   CE   NZ                                   
REMARK 470     PHE A 314    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 315    CG1  CG2  CD1                                       
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E  16    CG   CD   CE   NZ                                   
REMARK 470     GLU E  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  78    CG   CD   CE   NZ                                   
REMARK 470     LYS E  83    CE   NZ                                             
REMARK 470     GLU E  86    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 165    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E 166    CG   OD1  OD2                                       
REMARK 470     LYS E 168    CG   CD   CE   NZ                                   
REMARK 470     GLN E 176    CG   CD   OE1  NE2                                  
REMARK 470     PHE E 185    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS E 199    SG                                                  
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 279    CG   CD   CE   NZ                                   
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 295    CD   CE   NZ                                        
REMARK 470     PHE E 314    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE E 315    CG1  CG2  CD1                                       
REMARK 470     LYS E 317    CG   CD   CE   NZ                                   
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR E 164   CE1   TYR E 164   CZ      0.095                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  36       70.66     50.44                                   
REMARK 500    ALA A  38     -170.37   -174.96                                   
REMARK 500    ILE A  46      -61.94    -96.65                                   
REMARK 500    ARG A 165      -71.89     74.17                                   
REMARK 500    ASP A 184       66.58     33.76                                   
REMARK 500    ASN A 216     -179.74   -172.02                                   
REMARK 500    ASP A 241      -70.68    -65.52                                   
REMARK 500    SER A 259      -34.47    -32.20                                   
REMARK 500    LEU A 273       46.25    -87.92                                   
REMARK 500    ASP A 276       95.50    -63.12                                   
REMARK 500    ARG A 308       16.33     82.15                                   
REMARK 500    ASN E  36       71.74     46.23                                   
REMARK 500    ILE E  46      -66.54    -94.41                                   
REMARK 500    ARG E 165      -78.98     73.48                                   
REMARK 500    ASP E 184       65.83     34.83                                   
REMARK 500    LYS E 217      -31.94    -33.20                                   
REMARK 500    ASP E 241      -70.42    -64.80                                   
REMARK 500    SER E 259      -34.42    -34.68                                   
REMARK 500    LEU E 273       48.42    -86.79                                   
REMARK 500    ASP E 276       96.25    -58.56                                   
REMARK 500    ARG E 308       14.02     81.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC SUBUNIT OF CAMP-DEPENDENT             
REMARK 900 PROTEIN KINASE COMPLEXED WITH ATP AND IP20.                          
REMARK 900 RELATED ID: 1J3H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO CAMP-DEPENDENT PROTEIN KINASE.              
DBREF  4DFY A    0   350  UNP    P05132   KAPCA_MOUSE      1    351             
DBREF  4DFY E    0   350  UNP    P05132   KAPCA_MOUSE      1    351             
SEQADV 4DFY MET A  -20  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY A  -19  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER A  -18  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER A  -17  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -16  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -15  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -14  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -13  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -12  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A  -11  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER A  -10  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER A   -9  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY A   -8  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY LEU A   -7  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY VAL A   -6  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY PRO A   -5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY ARG A   -4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY A   -3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER A   -2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS A   -1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY ALA A  194  UNP  P05132    ARG   195 ENGINEERED MUTATION            
SEQADV 4DFY MET E  -20  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY E  -19  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER E  -18  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER E  -17  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -16  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -15  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -14  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -13  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -12  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E  -11  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER E  -10  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER E   -9  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY E   -8  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY LEU E   -7  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY VAL E   -6  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY PRO E   -5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY ARG E   -4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY GLY E   -3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY SER E   -2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY HIS E   -1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DFY ALA E  194  UNP  P05132    ARG   195 ENGINEERED MUTATION            
SEQRES   1 A  371  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  371  LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA          
SEQRES   3 A  371  ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE          
SEQRES   4 A  371  LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU          
SEQRES   5 A  371  THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP          
SEQRES   6 A  371  ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL          
SEQRES   7 A  371  MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA          
SEQRES   8 A  371  MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS          
SEQRES   9 A  371  GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN          
SEQRES  10 A  371  ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER          
SEQRES  11 A  371  PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR          
SEQRES  12 A  371  VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE          
SEQRES  13 A  371  GLY ARG PHE SER GLU PRO HIS ALA ARG PHE TYR ALA ALA          
SEQRES  14 A  371  GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP          
SEQRES  15 A  371  LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE          
SEQRES  16 A  371  ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE          
SEQRES  17 A  371  ALA LYS ARG VAL LYS GLY ALA THR TRP THR LEU CYS GLY          
SEQRES  18 A  371  THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS          
SEQRES  19 A  371  GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL          
SEQRES  20 A  371  LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE          
SEQRES  21 A  371  ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER          
SEQRES  22 A  371  GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU          
SEQRES  23 A  371  LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR          
SEQRES  24 A  371  LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE          
SEQRES  25 A  371  LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA          
SEQRES  26 A  371  ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS          
SEQRES  27 A  371  PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR          
SEQRES  28 A  371  GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS          
SEQRES  29 A  371  GLY LYS GLU PHE THR GLU PHE                                  
SEQRES   1 E  371  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  371  LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA          
SEQRES   3 E  371  ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE          
SEQRES   4 E  371  LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU          
SEQRES   5 E  371  THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP          
SEQRES   6 E  371  ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL          
SEQRES   7 E  371  MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA          
SEQRES   8 E  371  MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS          
SEQRES   9 E  371  GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN          
SEQRES  10 E  371  ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER          
SEQRES  11 E  371  PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR          
SEQRES  12 E  371  VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE          
SEQRES  13 E  371  GLY ARG PHE SER GLU PRO HIS ALA ARG PHE TYR ALA ALA          
SEQRES  14 E  371  GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP          
SEQRES  15 E  371  LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE          
SEQRES  16 E  371  ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE          
SEQRES  17 E  371  ALA LYS ARG VAL LYS GLY ALA THR TRP THR LEU CYS GLY          
SEQRES  18 E  371  THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS          
SEQRES  19 E  371  GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL          
SEQRES  20 E  371  LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE          
SEQRES  21 E  371  ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER          
SEQRES  22 E  371  GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU          
SEQRES  23 E  371  LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR          
SEQRES  24 E  371  LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE          
SEQRES  25 E  371  LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA          
SEQRES  26 E  371  ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS          
SEQRES  27 E  371  PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR          
SEQRES  28 E  371  GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS          
SEQRES  29 E  371  GLY LYS GLU PHE THR GLU PHE                                  
MODRES 4DFY SEP A  338  SER  PHOSPHOSERINE                                      
MODRES 4DFY SEP E  338  SER  PHOSPHOSERINE                                      
HET    SEP  A 338      10                                                       
HET    SEP  E 338      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  HOH   *7(H2 O)                                                      
HELIX    1   1 SER A   14  THR A   32  1                                  19    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  VAL A   98  1                                  15    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SER A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  LEU A  211  1                                   6    
HELIX   10  10 ALA A  218  GLY A  234  1                                  17    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 ASP A  276  ARG A  280  5                                   5    
HELIX   14  14 VAL A  288  HIS A  294  1                                   7    
HELIX   15  15 LYS A  295  ALA A  298  5                                   4    
HELIX   16  16 ASP A  301  ARG A  308  1                                   8    
HELIX   17  17 VAL E   15  THR E   32  1                                  18    
HELIX   18  18 GLN E   39  ASP E   41  5                                   3    
HELIX   19  19 LYS E   76  LEU E   82  1                                   7    
HELIX   20  20 GLN E   84  VAL E   98  1                                  15    
HELIX   21  21 GLU E  127  GLY E  136  1                                  10    
HELIX   22  22 SER E  139  LEU E  160  1                                  22    
HELIX   23  23 LYS E  168  GLU E  170  5                                   3    
HELIX   24  24 THR E  201  LEU E  205  5                                   5    
HELIX   25  25 ALA E  206  LEU E  211  1                                   6    
HELIX   26  26 ALA E  218  GLY E  234  1                                  17    
HELIX   27  27 GLN E  242  GLY E  253  1                                  12    
HELIX   28  28 SER E  262  LEU E  273  1                                  12    
HELIX   29  29 ASP E  276  ARG E  280  5                                   5    
HELIX   30  30 VAL E  288  ASN E  293  1                                   6    
HELIX   31  31 HIS E  294  ALA E  298  5                                   5    
HELIX   32  32 ASP E  301  ARG E  308  1                                   8    
HELIX   33  33 GLY E  344  THR E  348  5                                   5    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  VAL A  57   N  GLY A  50           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  TYR A  69   N  VAL A  60           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   B 2 LEU A 172  ILE A 174  0                                        
SHEET    2   B 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1   C 5 PHE E  43  THR E  51  0                                        
SHEET    2   C 5 ARG E  56  HIS E  62 -1  O  VAL E  57   N  GLY E  50           
SHEET    3   C 5 HIS E  68  ASP E  75 -1  O  MET E  71   N  MET E  58           
SHEET    4   C 5 ASN E 115  GLU E 121 -1  O  MET E 118   N  LYS E  72           
SHEET    5   C 5 LEU E 106  LYS E 111 -1  N  PHE E 108   O  VAL E 119           
SHEET    1   D 2 LEU E 172  ILE E 174  0                                        
SHEET    2   D 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.32  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.34  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
CRYST1   95.745   95.745  173.959  90.00  90.00 120.00 P 32 2 1     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      0.010444  0.006030  0.000000        0.00000                         
SCALE2      0.000000  0.012060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005748        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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