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Database: PDB
Entry: 4DG0
LinkDB: 4DG0
Original site: 4DG0 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-JAN-12   4DG0              
TITLE     CRYSTAL STRUCTURE OF MYRISTOYLATED WT CATALYTIC SUBUNIT OF CAMP-      
TITLE    2 DEPENDENT PROTEIN KINASE IN COMPLEX WITH SP20 AND AMP-PNP            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2-351;                                        
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 6-25;                                         
COMPND  12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  13 MUSCLE/BRAIN ISOFORM;                                                
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 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                                                
KEYWDS    PROTEIN KINASE, MYRISTOYLATED, PHOSPHOTRANSFERASE OF SER/THR, MG,     
KEYWDS   2 PKI, PKA REGULATORY SUBUNITS, PHOSPHORYLATED ON S139, T197, S338,    
KEYWDS   3 MYRISTOYLATED ON G1, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.M.STEICHEN,S.S.TAYLOR                                  
REVDAT   2   02-JAN-13 4DG0    1       JRNL                                     
REVDAT   1   06-JUN-12 4DG0    0                                                
JRNL        AUTH   A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,M.M.KESHWANI,Y.GUO,       
JRNL        AUTH 2 S.S.TAYLOR                                                   
JRNL        TITL   ROLE OF N-TERMINAL MYRISTYLATION IN THE STRUCTURE AND        
JRNL        TITL 2 REGULATION OF CAMP-DEPENDENT PROTEIN KINASE.                 
JRNL        REF    J.MOL.BIOL.                   V. 422   215 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22617327                                                     
JRNL        DOI    10.1016/J.JMB.2012.05.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 29601                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1572                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2165                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2951                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 344                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
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): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.156         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.302         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3096 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4190 ; 0.951 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   369 ; 4.529 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;34.244 ;23.933       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   545 ;12.971 ;15.055       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;15.595 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   441 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2322 ; 0.003 ; 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):  1810 ; 0.232 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2920 ; 0.444 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1286 ; 0.593 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1265 ; 0.996 ; 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 : 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    10        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3317 -13.5081  21.0208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0042 T22:   0.0311                                     
REMARK   3      T33:   0.0743 T12:   0.0015                                     
REMARK   3      T13:   0.0024 T23:   0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4681 L22:   1.1342                                     
REMARK   3      L33:   2.2173 L12:  -0.0323                                     
REMARK   3      L13:   0.2103 L23:   0.7866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:   0.0024 S13:   0.0082                       
REMARK   3      S21:   0.0273 S22:  -0.0067 S23:   0.0557                       
REMARK   3      S31:   0.0175 S32:  -0.0105 S33:   0.0202                       
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    24                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0853  -2.4947  26.2690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:   0.0475                                     
REMARK   3      T33:   0.0502 T12:  -0.0011                                     
REMARK   3      T13:   0.0074 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0923 L22:   6.4736                                     
REMARK   3      L33:   6.2554 L12:   2.5318                                     
REMARK   3      L13:   2.4898 L23:   4.3371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.1346 S13:  -0.1904                       
REMARK   3      S21:   0.0304 S22:   0.1666 S23:  -0.4190                       
REMARK   3      S31:   0.2849 S32:   0.2854 S33:  -0.1390                       
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   402        E   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7369  -8.4045  13.9098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0827 T22:   0.1160                                     
REMARK   3      T33:   0.0686 T12:   0.0103                                     
REMARK   3      T13:  -0.0131 T23:  -0.0395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1953 L22:   7.7681                                     
REMARK   3      L33:   6.6145 L12:   2.7857                                     
REMARK   3      L13:   1.6212 L23:   1.4061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1000 S12:   0.0044 S13:  -0.1839                       
REMARK   3      S21:  -0.5048 S22:   0.2296 S23:  -0.4522                       
REMARK   3      S31:  -0.0852 S32:  -0.2311 S33:  -0.1297                       
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   501        E   731                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2980 -12.2726  19.4716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0669 T22:   0.1070                                     
REMARK   3      T33:   0.1238 T12:  -0.0032                                     
REMARK   3      T13:   0.0121 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3526 L22:   0.7526                                     
REMARK   3      L33:   1.5628 L12:   0.0840                                     
REMARK   3      L13:   0.2960 L23:   0.4030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0263 S12:  -0.0236 S13:   0.0136                       
REMARK   3      S21:   0.0052 S22:  -0.0301 S23:   0.0562                       
REMARK   3      S31:   0.0142 S32:  -0.0026 S33:   0.0564                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
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):  -2.5390 -13.6204  15.9170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0498 T22:   0.1079                                     
REMARK   3      T33:   0.1365 T12:  -0.0032                                     
REMARK   3      T13:  -0.0428 T23:   0.1064                                     
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 : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   404        E   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8390 -10.0623  17.0670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0733 T22:   0.0126                                     
REMARK   3      T33:   0.0898 T12:  -0.0246                                     
REMARK   3      T13:  -0.0633 T23:   0.0336                                     
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 4DG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070281.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAY-11                          
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                       : 8.2.1                              
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31277                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 10% MPD   PROTEIN         
REMARK 280  SOLUTION: 50 MM BICINE, 150 MM AMMONIUM ACETATE, 8-10 MG/ML 9%      
REMARK 280  MEOH ADDED TO THE WELL IMMEDIATELY BEFORE SEALING. 8 UL DROP SIZE   
REMARK 280  WITH 1:1 PROTEIN:MOTHER LIQUOR, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  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       28.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.50000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.36500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.50000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.36500            
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: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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     GLU E  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN E  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  13    CG   CD   OE1  OE2                                  
REMARK 470     SER E  14    OG                                                  
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
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    HIS E  87   NE2   HIS E  87   CD2    -0.067                       
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     -162.28   -126.67                                   
REMARK 500    ASP E 166       45.63   -146.43                                   
REMARK 500    ASP E 184       79.89     65.44                                   
REMARK 500    LYS E 319       56.06    -97.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 513        DISTANCE =  6.44 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYR E  401                                                       
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 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 402   O3G                                                    
REMARK 620 2 HOH E 597   O   112.2                                              
REMARK 620 3 ANP E 402   O1B  86.0 102.1                                        
REMARK 620 4 HOH E 598   O   100.0  87.3 166.2                                  
REMARK 620 5 ASP E 184   OD1 147.8  99.4  81.5  87.0                            
REMARK 620 6 ASP E 184   OD2  93.9 153.5  83.5  83.7  55.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 402   O2G                                                    
REMARK 620 2 ANP E 402   O2A 147.9                                              
REMARK 620 3 ASN E 171   OD1 114.6  96.7                                        
REMARK 620 4 HOH E 599   O   101.5  88.0  84.5                                  
REMARK 620 5 ASP E 184   OD2  85.4  88.1  89.2 172.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP 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 RESIDUE MG E 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
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: 4DFX   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX WITH MYR-K7C                                            
REMARK 900 RELATED ID: 4DFZ   RELATED DB: PDB                                   
REMARK 900 MYR-K7C IN COMPLEX WITH SP20                                         
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ATP AND IP20.           
REMARK 900 RELATED ID: 1JBP   RELATED DB: PDB                                   
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ADP AND SP20.           
REMARK 900 RELATED ID: 1CTP   RELATED DB: PDB                                   
REMARK 900 MYRISTOYLATED CATALYTIC SUBUNIT OF PKA BOUND TO IP20.                
REMARK 900 RELATED ID: 4DG2   RELATED DB: PDB                                   
DBREF  4DG0 E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4DG0 I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4DG0 ALA I   20  UNP  P63248    ASN    21 ENGINEERED MUTATION            
SEQADV 4DG0 SER 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 SEP 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 SER ILE HIS ASP                                  
MODRES 4DG0 SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 4DG0 TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 4DG0 SEP E  338  SER  PHOSPHOSERINE                                      
HET    SEP  E 139      10                                                       
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    MYR  E 401      15                                                       
HET    ANP  E 402      31                                                       
HET     MG  E 403       1                                                       
HET     MG  E 404       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  MYR    C14 H28 O2                                                   
FORMUL   4  ANP    C10 H17 N6 O12 P3                                            
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *344(H2 O)                                                    
HELIX    1   1 GLN E   12  THR E   32  1                                  21    
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 SEP 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  GLY E  253  1                                  12    
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  ALA I   12  1                                   7    
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  PHE E 110   O  TYR E 117           
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   PHE E 138                 N   SEP E 139     1555   1555  1.33  
LINK         C   SEP E 139                 N   GLU E 140     1555   1555  1.33  
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         O3G ANP E 402                MG    MG E 403     1555   1555  1.93  
LINK         O2G ANP E 402                MG    MG E 404     1555   1555  1.93  
LINK        MG    MG E 403                 O   HOH E 597     1555   1555  1.96  
LINK         O1B ANP E 402                MG    MG E 403     1555   1555  2.05  
LINK         O2A ANP E 402                MG    MG E 404     1555   1555  2.06  
LINK         OD1 ASN E 171                MG    MG E 404     1555   1555  2.16  
LINK        MG    MG E 404                 O   HOH E 599     1555   1555  2.19  
LINK         OD2 ASP E 184                MG    MG E 404     1555   1555  2.25  
LINK        MG    MG E 403                 O   HOH E 598     1555   1555  2.29  
LINK         OD1 ASP E 184                MG    MG E 403     1555   1555  2.34  
LINK         OD2 ASP E 184                MG    MG E 403     1555   1555  2.38  
CISPEP   1 HIS I   23    ASP I   24          0         0.18                     
SITE     1 AC1  1 GLU E 155                                                     
SITE     1 AC2 28 GLY E  52  VAL E  57  ALA E  70  LYS E  72                    
SITE     2 AC2 28 VAL E 104  MET E 120  GLU E 121  TYR E 122                    
SITE     3 AC2 28 VAL E 123  GLU E 127  ASP E 166  LYS E 168                    
SITE     4 AC2 28 GLU E 170  ASN E 171  LEU E 173  THR E 183                    
SITE     5 AC2 28 ASP E 184  PHE E 327   MG E 403   MG E 404                    
SITE     6 AC2 28 HOH E 521  HOH E 522  HOH E 599  HOH E 642                    
SITE     7 AC2 28 HOH E 748  HOH E 751  ARG I  18  SER I  21                    
SITE     1 AC3  4 ASP E 184  ANP E 402  HOH E 597  HOH E 598                    
SITE     1 AC4  4 ASN E 171  ASP E 184  ANP E 402  HOH E 599                    
SITE     1 AC5 63 LEU E  82  GLN E  84  GLU E  86  HIS E  87                    
SITE     2 AC5 63 LEU E  89  ARG E  93  GLU E 127  PHE E 129                    
SITE     3 AC5 63 ARG E 133  ASP E 166  LYS E 168  PRO E 169                    
SITE     4 AC5 63 GLU E 170  PHE E 187  LYS E 189  ARG E 190                    
SITE     5 AC5 63 VAL E 191  LYS E 192  TPO E 197  LEU E 198                    
SITE     6 AC5 63 CYS E 199  GLY E 200  GLU E 203  GLU E 230                    
SITE     7 AC5 63 TYR E 235  PRO E 236  PHE E 239  ALA E 240                    
SITE     8 AC5 63 ASP E 241  PRO E 243  TYR E 330  GLU E 349                    
SITE     9 AC5 63 ANP E 402  HOH E 513  HOH E 514  HOH E 518                    
SITE    10 AC5 63 HOH E 523  HOH E 594  HOH E 608  HOH E 735                    
SITE    11 AC5 63 HOH I 101  HOH I 102  HOH I 103  HOH I 104                    
SITE    12 AC5 63 HOH I 105  HOH I 106  HOH I 107  HOH I 108                    
SITE    13 AC5 63 HOH I 109  HOH I 111  HOH I 112  HOH I 114                    
SITE    14 AC5 63 HOH I 115  HOH I 116  HOH I 117  HOH I 118                    
SITE    15 AC5 63 HOH I 119  HOH I 121  HOH I 124  HOH I 126                    
SITE    16 AC5 63 HOH I 127  HOH I 130  HOH I 131                               
CRYST1   57.800   78.730   99.000  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      0.017301  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010101        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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