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Database: PDB
Entry: 4HPT
LinkDB: 4HPT
Original site: 4HPT 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-OCT-12   4HPT              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN  
TITLE    2 KINASE DISPLAYING COMPLETE PHOSPHORYL TRANSFER OF AMP-PNP ONTO A     
TITLE    3 SUBSTRATE PEPTIDE                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND   9 CHAIN: I;                                                            
COMPND  10 FRAGMENT: SP20 DERIVED FROM PKI (UNP RESIDUES 6-25);                 
COMPND  11 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  12 MUSCLE/BRAIN ISOFORM;                                                
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 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;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    PROTEIN KINASE, PHOSPHOTRANSFERASE, REGULATORY SUBUNITS, PKI,         
KEYWDS   2 MAGNESIUM, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR        
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.M.STEICHEN,J.WU,S.S.TAYLOR                             
REVDAT   4   15-NOV-17 4HPT    1       REMARK                                   
REVDAT   3   10-APR-13 4HPT    1       JRNL                                     
REVDAT   2   27-MAR-13 4HPT    1       JRNL                                     
REVDAT   1   20-MAR-13 4HPT    0                                                
JRNL        AUTH   A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,Y.GUO,J.WU,S.S.TAYLOR     
JRNL        TITL   PHOSPHORYL TRANSFER BY PROTEIN KINASE A IS CAPTURED IN A     
JRNL        TITL 2 CRYSTAL LATTICE.                                             
JRNL        REF    J.AM.CHEM.SOC.                V. 135  4788 2013              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23458248                                                     
JRNL        DOI    10.1021/JA312237Q                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20161                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1076                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1098                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : 1.98000                                              
REMARK   3    B33 (A**2) : -1.84000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.277         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.208         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.412        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3018 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4089 ; 1.155 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   358 ; 5.512 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   147 ;35.923 ;23.878       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   522 ;14.545 ;15.057       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.757 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   433 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2280 ; 0.005 ; 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):  1776 ; 0.497 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2864 ; 0.936 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1242 ; 1.344 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1223 ; 2.201 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    14        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0983  -2.5511  -2.5763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0041 T22:   0.0602                                     
REMARK   3      T33:   0.0196 T12:  -0.0093                                     
REMARK   3      T13:  -0.0023 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2947 L22:   0.6288                                     
REMARK   3      L33:   0.9711 L12:  -0.2414                                     
REMARK   3      L13:   0.0375 L23:   0.2677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0010 S12:   0.0076 S13:   0.0208                       
REMARK   3      S21:  -0.0103 S22:  -0.0145 S23:   0.0125                       
REMARK   3      S31:  -0.0151 S32:   0.1377 S33:   0.0135                       
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 :   I     5        I    23                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7290   1.1935   9.2946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0611 T22:   0.0606                                     
REMARK   3      T33:   0.0209 T12:  -0.0223                                     
REMARK   3      T13:   0.0065 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7121 L22:   1.6413                                     
REMARK   3      L33:   2.7390 L12:  -0.9867                                     
REMARK   3      L13:  -0.5716 L23:   1.8433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0820 S12:  -0.0896 S13:  -0.0985                       
REMARK   3      S21:  -0.0646 S22:   0.0218 S23:   0.0920                       
REMARK   3      S31:  -0.0125 S32:  -0.1422 S33:   0.0602                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   401        E   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5930 -10.1383   2.5248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0242 T22:   0.1567                                     
REMARK   3      T33:   0.0884 T12:  -0.0277                                     
REMARK   3      T13:  -0.0040 T23:   0.0525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8988 L22:  27.6818                                     
REMARK   3      L33:   0.1838 L12: -10.3884                                     
REMARK   3      L13:  -0.8459 L23:   2.2533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1716 S12:  -0.0718 S13:   0.2778                       
REMARK   3      S21:   0.4920 S22:   0.2211 S23:  -0.7315                       
REMARK   3      S31:   0.0411 S32:   0.0094 S33:  -0.0495                       
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   402        E   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4696  -7.2082   0.5280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0550 T22:   0.0781                                     
REMARK   3      T33:   0.0585 T12:  -0.0254                                     
REMARK   3      T13:   0.0036 T23:   0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   501        E   659                          
REMARK   3    RESIDUE RANGE :   I   101        I   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5477  -2.2906  -1.3541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0410 T22:   0.0465                                     
REMARK   3      T33:   0.0573 T12:   0.0097                                     
REMARK   3      T13:   0.0002 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6696 L22:   0.3291                                     
REMARK   3      L33:   1.0758 L12:  -0.3965                                     
REMARK   3      L13:  -0.1794 L23:   0.3962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0213 S12:   0.0114 S13:  -0.0020                       
REMARK   3      S21:   0.0056 S22:   0.0035 S23:   0.0176                       
REMARK   3      S31:   0.0174 S32:   0.0808 S33:   0.0178                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   403        E   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0937  -8.5463  -3.3910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.2109                                     
REMARK   3      T33:   0.2470 T12:  -0.0718                                     
REMARK   3      T13:   0.0368 T23:   0.1783                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
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 4HPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075768.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: MOLECULAR REPLACEMENT                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 50 MM BICINE, 150 MM     
REMARK 280  AMMONIUM ACETATE, 10 MM DTT, ~7-10 MG/ML PROTEIN WELL SOLUTION:     
REMARK 280  1 ML OF 2% MPD, 80 UL METHANOL ADDED TO THE WELL IMMEDIATELY        
REMARK 280  BEFORE SEALING 8 UL DROPS OF 1:1 PROTEIN:WELL WERE USED., VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.15K, PH 8.0                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.77250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.04500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.04500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.77250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.53000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY 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     ASP I    24                                                      
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 E  16    CE   NZ                                             
REMARK 470     LYS E 105    CD   CE   NZ                                        
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 317    CE   NZ                                             
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH E   548     O    HOH E   655              2.01            
REMARK 500   O    LYS E   213     O    HOH E   643              2.07            
REMARK 500   O    HOH E   609     O    HOH E   630              2.14            
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    ASP E 112     -154.85   -130.43                                   
REMARK 500    ASP E 166       38.25   -142.90                                   
REMARK 500    ASP E 184       81.09     67.73                                   
REMARK 500    LEU E 273       48.56    -86.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 401   N3B                                                    
REMARK 620 2 ANP E 401   O2A  80.0                                              
REMARK 620 3 HOH I 104   O    88.0 162.1                                        
REMARK 620 4 ASN E 171   OD1 172.7  92.8  99.1                                  
REMARK 620 5 HOH E 520   O    89.5  90.4 102.8  90.0                            
REMARK 620 6 ASP E 184   OD2  86.9  87.1  78.9  93.2 176.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP I  21   O1P                                                    
REMARK 620 2 ANP E 401   O1B  87.7                                              
REMARK 620 3 HOH E 519   O    83.5 152.1                                        
REMARK 620 4 HOH I 101   O    93.2 115.2  91.8                                  
REMARK 620 5 ASP E 184   OD1 123.4  87.7  75.4 138.4                            
REMARK 620 6 ASP E 184   OD2  75.3  74.9  77.2 164.8  49.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT         
REMARK 800  PROTEIN KINASE INHIBITOR ALPHA                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH IP20                                    
REMARK 900 RELATED ID: 1L3R   RELATED DB: PDB                                   
REMARK 900 TRANSITION STATE MIMIC OF SAME PROTEIN IN COMPLEX WITH THE SAME      
REMARK 900 SUBSTRATE PEPTIDE                                                    
REMARK 900 RELATED ID: 4DFX   RELATED DB: PDB                                   
REMARK 900 MYRISTYLATED CATALYTIC SUBUNIT WITH A K7C MUTATION IN COMPLEX WITH   
REMARK 900 AMP-PNP AND THE SAME SUBSTRATE PEPTIDE WITHOUT TRANSFER              
REMARK 900 RELATED ID: 4DG0   RELATED DB: PDB                                   
REMARK 900 MYRISTYLATED CATALYTIC SUBUNIT IN COMPLEX WITH AMP-PNP AND THE SAME  
REMARK 900 SUBSTRATE PEPTIDE WITHOUT TRANSFER                                   
REMARK 900 RELATED ID: 1JLU   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN A COMPLEX WITH THE SAME SUBSTRATE PEPTIDE THAT WAS   
REMARK 900 PHOSPHORYLATED PRIOR TO CRYSTALLIZATION                              
REMARK 900 RELATED ID: 1JBP   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH THE SAME SUBSTRATE PEPTIDE AND ADP      
REMARK 900 RELATED ID: 4DH1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE SAME PROTEIN WITH LOW MAGNESIUM SHOWING OCCUPANCY   
REMARK 900 OF ONLY ONE MAGNESIUM SITE, MG2.                                     
REMARK 900 RELATED ID: 4HPU   RELATED DB: PDB                                   
DBREF  4HPT E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4HPT I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4HPT ALA I   20  UNP  P63248    ASN    21 ENGINEERED MUTATION            
SEQADV 4HPT SEP I   21  UNP  P63248    ALA    22 ENGINEERED MUTATION            
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 E  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 E  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 E  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 E  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 E  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 E  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 E  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 E  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 E  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 E  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 E  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 E  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 E  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 E  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 E  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ALA SEP ILE HIS ASP                                  
MODRES 4HPT TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 4HPT SEP E  338  SER  PHOSPHOSERINE                                      
MODRES 4HPT SEP I   21  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    SEP  I  21      10                                                       
HET    ANP  E 401      27                                                       
HET     MG  E 402       1                                                       
HET     MG  E 403       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *177(H2 O)                                                    
HELIX    1   1 SER E   14  THR E   32  1                                  19    
HELIX    2   2 GLN E   39  ASP E   41  5                                   3    
HELIX    3   3 LYS E   76  LEU E   82  1                                   7    
HELIX    4   4 GLN E   84  GLN E   96  1                                  13    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SER E  139  LEU E  160  1                                  22    
HELIX    7   7 LYS E  168  GLU E  170  5                                   3    
HELIX    8   8 THR E  201  LEU E  205  5                                   5    
HELIX    9   9 ALA E  206  LEU E  211  1                                   6    
HELIX   10  10 LYS E  217  GLY E  234  1                                  18    
HELIX   11  11 GLN E  242  SER E  252  1                                  11    
HELIX   12  12 SER E  262  LEU E  273  1                                  12    
HELIX   13  13 VAL E  288  ASN E  293  1                                   6    
HELIX   14  14 HIS E  294  ALA E  298  5                                   5    
HELIX   15  15 ASP E  301  GLN E  307  1                                   7    
HELIX   16  16 THR I    6  SER I   13  1                                   8    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 GLY E  55  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  ILE E  73   N  ARG E  56           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 118   N  LYS E  72           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  GLU E 107   O  VAL E 119           
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   C 2 LEU E 172  ILE E 174  0                                        
SHEET    2   C 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.33  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.33  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
LINK         C   ALA I  20                 N   SEP I  21     1555   1555  1.33  
LINK         C   SEP I  21                 N   ILE I  22     1555   1555  1.32  
LINK         N3B ANP E 401                MG    MG E 402     1555   1555  2.02  
LINK         O2A ANP E 401                MG    MG E 402     1555   1555  2.05  
LINK         O1P SEP I  21                MG    MG E 403     1555   1555  2.10  
LINK         O1B ANP E 401                MG    MG E 403     1555   1555  2.15  
LINK        MG    MG E 402                 O   HOH I 104     1555   1555  2.16  
LINK         OD1 ASN E 171                MG    MG E 402     1555   1555  2.17  
LINK        MG    MG E 402                 O   HOH E 520     1555   1555  2.27  
LINK         OD2 ASP E 184                MG    MG E 402     1555   1555  2.28  
LINK        MG    MG E 403                 O   HOH E 519     1555   1555  2.30  
LINK        MG    MG E 403                 O   HOH I 101     1555   1555  2.42  
LINK         OD1 ASP E 184                MG    MG E 403     1555   1555  2.51  
LINK         OD2 ASP E 184                MG    MG E 403     1555   1555  2.74  
SITE     1 AC1 26 GLY E  50  GLY E  52  VAL E  57  ALA E  70                    
SITE     2 AC1 26 LYS E  72  VAL E 104  MET E 120  GLU E 121                    
SITE     3 AC1 26 TYR E 122  VAL E 123  GLU E 127  GLU E 170                    
SITE     4 AC1 26 ASN E 171  LEU E 173  THR E 183  ASP E 184                    
SITE     5 AC1 26 PHE E 327   MG E 402   MG E 403  HOH E 520                    
SITE     6 AC1 26 HOH E 556  HOH E 594  HOH E 646  ARG I  18                    
SITE     7 AC1 26 SEP I  21  HOH I 104                                          
SITE     1 AC2  5 ASN E 171  ASP E 184  ANP E 401  HOH E 520                    
SITE     2 AC2  5 HOH I 104                                                     
SITE     1 AC3  5 ASP E 184  ANP E 401  HOH E 519  SEP I  21                    
SITE     2 AC3  5 HOH I 101                                                     
SITE     1 AC4 53 SER E  53  GLN E  84  GLU E  86  ARG E  93                    
SITE     2 AC4 53 GLU E 127  PHE E 129  ARG E 133  ASP E 166                    
SITE     3 AC4 53 LYS E 168  PRO E 169  GLU E 170  ASP E 184                    
SITE     4 AC4 53 PHE E 187  ARG E 190  LYS E 192  LEU E 198                    
SITE     5 AC4 53 CYS E 199  GLY E 200  PRO E 202  GLU E 203                    
SITE     6 AC4 53 GLU E 230  TYR E 235  PRO E 236  PHE E 239                    
SITE     7 AC4 53 ALA E 240  ASP E 241  ILE E 246  TYR E 330                    
SITE     8 AC4 53 GLU E 349  ANP E 401   MG E 403  HOH E 519                    
SITE     9 AC4 53 HOH E 530  HOH E 544  HOH E 558  HOH E 576                    
SITE    10 AC4 53 HOH E 596  HOH E 603  HOH E 622  HOH I 101                    
SITE    11 AC4 53 HOH I 102  HOH I 103  HOH I 104  HOH I 105                    
SITE    12 AC4 53 HOH I 106  HOH I 109  HOH I 110  HOH I 111                    
SITE    13 AC4 53 HOH I 112  HOH I 113  HOH I 114  HOH I 116                    
SITE    14 AC4 53 HOH I 117                                                     
CRYST1   71.545   79.060   80.090  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013977  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012649  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012486        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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