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Database: PDB
Entry: 3O7L
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Original site: 3O7L 
HEADER    TRANSFERASE                             30-JUL-10   3O7L              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOLAMBAN (1-19):PKA C-SUBUNIT:AMP-PNP:MG2+  
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: PHOSPHOLAMBAN PEPTIDE;                                     
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 CATALYTIC SUBUNIT ALPHA;     
COMPND  10 CHAIN: D;                                                            
COMPND  11 SYNONYM: PKA C-ALPHA;                                                
COMPND  12 EC: 2.7.11.11;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CARDIAC PHOSPHOLAMBAN;                                     
COMPND  16 CHAIN: I;                                                            
COMPND  17 SYNONYM: PLB;                                                        
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PKACA, PRKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: PKACA, PRKACA;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 OTHER_DETAILS: CHEMICALLY SYNTHESIZED. THIS SEQUENCE OCCURS          
SOURCE  18 NATURALLY FROM PHOSPHOLAMBAN                                         
KEYWDS    PROTEIN KINASE A, PHOSPHOLAMBAN, ALLOSTERY, SUBSTRATE RECOGNITION,    
KEYWDS   2 CONFORMATIONAL SELECTION, INTRINSICALLY DISORDERED PROTEINS,         
KEYWDS   3 MEMBRANE PROTEINS, TRANSFERASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.Y.CHENG,S.S.TAYLOR                                                  
REVDAT   2   01-DEC-10 3O7L    1       JRNL                                     
REVDAT   1   06-OCT-10 3O7L    0                                                
JRNL        AUTH   L.R.MASTERSON,C.CHENG,T.YU,M.TONELLI,A.KORNEV,S.S.TAYLOR,    
JRNL        AUTH 2 G.VEGLIA                                                     
JRNL        TITL   DYNAMICS CONNECT SUBSTRATE RECOGNITION TO CATALYSIS IN       
JRNL        TITL 2 PROTEIN KINASE A.                                            
JRNL        REF    NAT.CHEM.BIOL.                V.   6   821 2010              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   20890288                                                     
JRNL        DOI    10.1038/NCHEMBIO.452                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25304                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1327                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.0906 -  5.5491    1.00     2786   149  0.2219 0.2480        
REMARK   3     2  5.5491 -  4.4064    1.00     2788   142  0.1867 0.2485        
REMARK   3     3  4.4064 -  3.8500    0.99     2731   154  0.1895 0.2596        
REMARK   3     4  3.8500 -  3.4982    0.97     2681   152  0.2452 0.3288        
REMARK   3     5  3.4982 -  3.2476    0.99     2737   151  0.2601 0.3608        
REMARK   3     6  3.2476 -  3.0562    1.00     2758   148  0.2468 0.3292        
REMARK   3     7  3.0562 -  2.9032    1.00     2727   161  0.2501 0.3404        
REMARK   3     8  2.9032 -  2.8000    1.00     2767   137  0.2369 0.3589        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 39.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.66090                                              
REMARK   3    B22 (A**2) : 7.66090                                              
REMARK   3    B33 (A**2) : -15.32180                                            
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5297                                  
REMARK   3   ANGLE     :  0.951           7204                                  
REMARK   3   CHIRALITY :  0.068            802                                  
REMARK   3   PLANARITY :  0.004            923                                  
REMARK   3   DIHEDRAL  : 19.331           1782                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4702  32.0699   7.6142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2216 T22:   0.0088                                     
REMARK   3      T33:  -0.1157 T12:  -0.0080                                     
REMARK   3      T13:  -0.0067 T23:   0.2412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6884 L22:   1.0574                                     
REMARK   3      L33:   0.9496 L12:  -0.5333                                     
REMARK   3      L13:  -0.6581 L23:  -0.8000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1226 S12:   0.2745 S13:  -0.5068                       
REMARK   3      S21:  -0.4984 S22:  -0.1652 S23:   0.5459                       
REMARK   3      S31:   0.1614 S32:  -0.4599 S33:  -2.0574                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7343  37.3507  33.9139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0075 T22:   0.0553                                     
REMARK   3      T33:   0.0325 T12:  -0.0083                                     
REMARK   3      T13:  -0.0949 T23:  -0.1350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7369 L22:   0.5979                                     
REMARK   3      L33:   0.6067 L12:   0.0179                                     
REMARK   3      L13:  -0.2419 L23:   0.0577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0120 S12:  -0.3447 S13:   0.0730                       
REMARK   3      S21:   0.2708 S22:   0.2006 S23:  -0.0991                       
REMARK   3      S31:  -0.0629 S32:   0.2308 S33:   0.0203                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN I                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7467  32.7040  10.3398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0050 T22:   0.0328                                     
REMARK   3      T33:   0.1870 T12:  -0.0305                                     
REMARK   3      T13:   0.1205 T23:   0.1420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0719 L22:   0.0063                                     
REMARK   3      L33:   0.0130 L12:   0.0008                                     
REMARK   3      L13:  -0.0097 L23:  -0.0043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0190 S12:  -0.0120 S13:  -0.0314                       
REMARK   3      S21:   0.0395 S22:   0.0561 S23:   0.0293                       
REMARK   3      S31:   0.0099 S32:   0.0192 S33:   0.0619                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3O7L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060765.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26095                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 264629.000                         
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 10.500                             
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE COMPLEX WAS OBTAINED BY COMBINING    
REMARK 280  A 1:10:10:10 MOLAR RATIO MIXTURE OF PKA-C (7 MG/ML), PLN1-19,       
REMARK 280  MGCL2, AND AMP-PNP IN 20 MM SODIUM ACETATE (PH 6.5), 180 MM KCL,    
REMARK 280  AND 5 MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.06200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      128.12400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       96.09300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      160.15500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.03100            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, 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 B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PHE B    54                                                      
REMARK 465     ILE B   339                                                      
REMARK 465     ASN B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     LYS B   342                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     GLN D    12                                                      
REMARK 465     PHE D   318                                                      
REMARK 465     LYS D   319                                                      
REMARK 465     GLY D   320                                                      
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 B  17    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  18    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     ASP B  25    CG   OD1  OD2                                       
REMARK 470     PHE B  26    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     TRP B  30    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  30    CZ3  CH2                                            
REMARK 470     GLU B  31    CG   CD   OE1  OE2                                  
REMARK 470     THR B  32    OG1  CG2                                            
REMARK 470     SER B  34    OG                                                  
REMARK 470     GLN B  35    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  36    CG   OD1  ND2                                       
REMARK 470     GLN B  39    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  40    CG   CD1  CD2                                       
REMARK 470     ASP B  41    CG   OD1  OD2                                       
REMARK 470     ASP B  44    CG   OD1  OD2                                       
REMARK 470     ARG B  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  46    CG1  CG2  CD1                                       
REMARK 470     ARG B  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  60    CG1  CG2                                            
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     HIS B  62    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     GLU B  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  77    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  81    CG   CD   CE   NZ                                   
REMARK 470     LEU B  82    CG   CD1  CD2                                       
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     GLU B  86    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  92    CG   CD   CE   NZ                                   
REMARK 470     GLN B  96    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     PHE B 108    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 109    OG                                                  
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     ASP B 112    CG   OD1  OD2                                       
REMARK 470     ASN B 113    CG   OD1  ND2                                       
REMARK 470     GLU B 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 189    CG   CD   CE   NZ                                   
REMARK 470     ARG B 190    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 192    CG   CD   CE   NZ                                   
REMARK 470     LYS B 213    CG   CD   CE   NZ                                   
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ARG B 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     LYS B 317    CG   CD   CE   NZ                                   
REMARK 470     GLU B 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 335    CG1  CG2  CD1                                       
REMARK 470     ARG B 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS B 343    SG                                                  
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     GLU B 346    CG   CD   OE1  OE2                                  
REMARK 470     THR B 348    OG1  CG2                                            
REMARK 470     GLU B 349    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 350    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D  13    CG   CD   OE1  OE2                                  
REMARK 470     SER D  14    OG                                                  
REMARK 470     VAL D  15    CG1  CG2                                            
REMARK 470     LYS D  16    CG   CD   CE   NZ                                   
REMARK 470     GLU D  17    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  19    CG   CD1  CD2                                       
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  28    CG   CD   CE   NZ                                   
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  83    CG   CD   CE   NZ                                   
REMARK 470     ASN D  99    CG   OD1  ND2                                       
REMARK 470     GLU D 121    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 134    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 159    OG                                                  
REMARK 470     GLN D 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 189    CG   CD   CE   NZ                                   
REMARK 470     LYS D 192    CG   CD   CE   NZ                                   
REMARK 470     ARG D 194    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 217    CG   CD   CE   NZ                                   
REMARK 470     LYS D 254    CG   CD   CE   NZ                                   
REMARK 470     ARG D 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 283    CG   OD1  ND2                                       
REMARK 470     LYS D 285    CG   CD   CE   NZ                                   
REMARK 470     ASN D 286    CG   OD1  ND2                                       
REMARK 470     VAL D 288    CG1  CG2                                            
REMARK 470     LYS D 295    CG   CD   CE   NZ                                   
REMARK 470     THR D 299    OG1  CG2                                            
REMARK 470     ARG D 308    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 309    CG   CD   CE   NZ                                   
REMARK 470     GLU D 311    CG   CD   OE1  OE2                                  
REMARK 470     PHE D 314    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D 317    CG   CD   CE   NZ                                   
REMARK 470     THR D 324    OG1  CG2                                            
REMARK 470     SER D 325    OG                                                  
REMARK 470     ASN D 326    CG   OD1  ND2                                       
REMARK 470     ASP D 329    CG   OD1  OD2                                       
REMARK 470     GLU D 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 335    CG1  CG2  CD1                                       
REMARK 470     ARG D 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 339    CG1  CG2  CD1                                       
REMARK 470     LYS D 342    CG   CD   CE   NZ                                   
REMARK 470     CYS D 343    SG                                                  
REMARK 470     GLU D 349    CG   CD   OE1  OE2                                  
REMARK 470     VAL I   9    CG1  CG2                                            
REMARK 470     GLN I  10    CG   CD   OE1  NE2                                  
REMARK 470     THR I  22    OG1  CG2                                            
REMARK 470     ILE I  23    CG1  CG2  CD1                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     MET B   71   CE                                                  
REMARK 480     LYS B   76   CD   CE   NZ                                        
REMARK 480     ARG B   93   NE   CZ   NH1  NH2                                  
REMARK 480     ILE B  163   CD1                                                 
REMARK 480     ARG B  194   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B  279   CD   CE   NZ                                        
REMARK 480     LYS B  285   CD   CE   NZ                                        
REMARK 480     LYS D   23   CD   CE   NZ                                        
REMARK 480     GLU D   31   CG   CD   OE1  OE2                                  
REMARK 480     LYS D   47   CE   NZ                                             
REMARK 480     LYS D   76   CD   CE   NZ                                        
REMARK 480     LYS D  105   CE   NZ                                             
REMARK 480     GLU D  155   OE1  OE2                                            
REMARK 480     GLN D  177   CD   OE1  NE2                                       
REMARK 480     LYS D  213   CD   CE   NZ                                        
REMARK 480     LYS D  279   NZ                                                  
REMARK 480     ILE D  303   CD1                                                 
REMARK 480     LYS D  345   CD   CE   NZ                                        
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   OD2  ASP B   184     O2A  ANP B   354              1.94            
REMARK 500   N    ASP B    75     O4   PEG B   353              1.97            
REMARK 500   NH1  ARG D   165     O2P  TPO D   197              2.06            
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    THR B  32       55.89   -169.57                                   
REMARK 500    ASP B  41       30.14    -83.58                                   
REMARK 500    ARG B  45       97.95    -49.30                                   
REMARK 500    LYS B  63      -77.77    -54.60                                   
REMARK 500    PHE B 110      161.23    176.79                                   
REMARK 500    ASP B 112       42.24    -75.27                                   
REMARK 500    SER B 114       -9.90   -149.32                                   
REMARK 500    ASP B 166       29.66   -153.54                                   
REMARK 500    LYS B 168      152.44    169.66                                   
REMARK 500    ASP B 184       74.91     57.63                                   
REMARK 500    LEU B 273       52.41    -91.02                                   
REMARK 500    LEU B 284     -155.44   -109.26                                   
REMARK 500    ASN D  36       72.72     21.30                                   
REMARK 500    ALA D  38     -163.12   -168.10                                   
REMARK 500    PHE D 110      173.29    166.77                                   
REMARK 500    ASP D 112     -167.22   -107.01                                   
REMARK 500    ASP D 166       21.54   -151.64                                   
REMARK 500    LYS D 168      143.96    175.10                                   
REMARK 500    ASP D 184       96.96     73.91                                   
REMARK 500    CYS D 199      -38.18   -150.51                                   
REMARK 500    PHE D 238       70.56   -116.88                                   
REMARK 500    ALA D 240      141.00   -173.30                                   
REMARK 500    HIS D 260       30.21    -80.88                                   
REMARK 500    ASP D 276       94.46    -67.92                                   
REMARK 500    THR D 299       48.45    -90.47                                   
REMARK 500    LYS D 309       40.61    -98.04                                   
REMARK 500    THR D 324       41.48    -73.90                                   
REMARK 500    CYS D 343       52.99     26.43                                   
REMARK 500    ARG I  14        3.06    -65.60                                   
REMARK 500    THR I  22      103.54    -52.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     ANP B  354                                                       
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 B 351  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 184   OD1                                                    
REMARK 620 2 ANP B 354   O1B  69.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 352  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP B 354   O2A                                                    
REMARK 620 2 ASP B 184   OD2  61.1                                              
REMARK 620 3 ANP B 354   O1B  80.8  56.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 351                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 352                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 354                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE C-SUBUNIT OF PKA                            
DBREF  3O7L B    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3O7L D    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3O7L I    9    23  UNP    P61014   PPLA_MOUSE       4     18             
SEQADV 3O7L ILE B  173  UNP  P05132    LEU   174 CONFLICT                       
SEQADV 3O7L ILE B  211  UNP  P05132    LEU   212 CONFLICT                       
SEQRES   1 B  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 B  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 B  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 B  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 B  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 B  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 B  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 B  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 B  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 B  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 B  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 B  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 B  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 B  350  GLU ASN LEU ILE ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 B  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 B  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 B  350  ILE ILE ILE SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 B  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 B  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 B  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 B  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 B  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 B  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 B  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 B  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 B  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SER          
SEQRES  27 B  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 D  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 D  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 D  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 D  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 D  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 D  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 D  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 D  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 D  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 D  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 D  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 D  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 D  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 D  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 D  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 D  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 D  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 D  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 D  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 D  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 D  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 D  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 D  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 D  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 D  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 D  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 D  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   15  VAL GLN TYR LEU THR ARG SER ALA ILE ARG ARG ALA SER          
SEQRES   2 I   15  THR ILE                                                      
MODRES 3O7L TPO B  197  THR  PHOSPHOTHREONINE                                   
MODRES 3O7L TPO D  197  THR  PHOSPHOTHREONINE                                   
MODRES 3O7L SEP D  338  SER  PHOSPHOSERINE                                      
HET    TPO  B 197      11                                                       
HET    TPO  D 197      11                                                       
HET    SEP  D 338      10                                                       
HET     MG  B 351       1                                                       
HET     MG  B 352       1                                                       
HET    PEG  B 353       7                                                       
HET    ANP  B 354      27                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  PEG    C4 H10 O3                                                    
FORMUL   7  ANP    C10 H17 N6 O12 P3                                            
FORMUL   8  HOH   *21(H2 O)                                                     
HELIX    1   1 GLU B   17  GLU B   31  1                                  15    
HELIX    2   2 GLN B   39  PHE B   43  5                                   5    
HELIX    3   3 LYS B   76  LEU B   82  1                                   7    
HELIX    4   4 GLN B   84  GLN B   96  1                                  13    
HELIX    5   5 GLU B  127  GLY B  136  1                                  10    
HELIX    6   6 SER B  139  LEU B  160  1                                  22    
HELIX    7   7 LYS B  168  GLU B  170  5                                   3    
HELIX    8   8 THR B  201  LEU B  205  5                                   5    
HELIX    9   9 ALA B  206  SER B  212  1                                   7    
HELIX   10  10 LYS B  217  GLY B  234  1                                  18    
HELIX   11  11 GLN B  242  GLY B  253  1                                  12    
HELIX   12  12 SER B  262  LEU B  273  1                                  12    
HELIX   13  13 VAL B  288  ASN B  293  1                                   6    
HELIX   14  14 HIS B  294  ALA B  298  5                                   5    
HELIX   15  15 ASP B  301  ARG B  308  1                                   8    
HELIX   16  16 GLY B  344  THR B  348  5                                   5    
HELIX   17  17 GLU D   13  THR D   32  1                                  20    
HELIX   18  18 GLN D   39  ASP D   41  5                                   3    
HELIX   19  19 LYS D   76  LEU D   82  1                                   7    
HELIX   20  20 GLN D   84  GLN D   96  1                                  13    
HELIX   21  21 GLU D  127  GLY D  136  1                                  10    
HELIX   22  22 SER D  139  LEU D  160  1                                  22    
HELIX   23  23 LYS D  168  GLU D  170  5                                   3    
HELIX   24  24 ALA D  206  LEU D  211  1                                   6    
HELIX   25  25 LYS D  217  GLY D  234  1                                  18    
HELIX   26  26 GLN D  242  GLY D  253  1                                  12    
HELIX   27  27 SER D  262  LEU D  273  1                                  12    
HELIX   28  28 VAL D  288  HIS D  294  1                                   7    
HELIX   29  29 LYS D  295  ALA D  298  5                                   4    
HELIX   30  30 ASP D  301  GLN D  307  1                                   7    
HELIX   31  31 GLY D  344  THR D  348  5                                   5    
SHEET    1   A 5 LYS B  47  GLY B  50  0                                        
SHEET    2   A 5 ARG B  56  LYS B  61 -1  O  VAL B  57   N  LEU B  49           
SHEET    3   A 5 HIS B  68  ASP B  75 -1  O  MET B  71   N  MET B  58           
SHEET    4   A 5 ASN B 115  GLU B 121 -1  O  LEU B 116   N  LEU B  74           
SHEET    5   A 5 LEU B 106  LYS B 111 -1  N  PHE B 108   O  VAL B 119           
SHEET    1   B 2 LEU B 162  ILE B 163  0                                        
SHEET    2   B 2 LYS B 189  ARG B 190 -1  O  LYS B 189   N  ILE B 163           
SHEET    1   C 2 LEU B 172  ILE B 174  0                                        
SHEET    2   C 2 ILE B 180  VAL B 182 -1  O  GLN B 181   N  ILE B 173           
SHEET    1   D 5 PHE D  43  THR D  51  0                                        
SHEET    2   D 5 GLY D  55  HIS D  62 -1  O  LEU D  59   N  LYS D  47           
SHEET    3   D 5 HIS D  68  ASP D  75 -1  O  MET D  71   N  MET D  58           
SHEET    4   D 5 ASN D 115  GLU D 121 -1  O  MET D 120   N  ALA D  70           
SHEET    5   D 5 LEU D 106  LYS D 111 -1  N  PHE D 108   O  VAL D 119           
SHEET    1   E 2 LEU D 162  ILE D 163  0                                        
SHEET    2   E 2 LYS D 189  ARG D 190 -1  O  LYS D 189   N  ILE D 163           
SHEET    1   F 2 LEU D 172  ILE D 174  0                                        
SHEET    2   F 2 ILE D 180  VAL D 182 -1  O  GLN D 181   N  LEU D 173           
LINK         C   TRP B 196                 N   TPO B 197     1555   1555  1.33  
LINK         C   TPO B 197                 N   LEU B 198     1555   1555  1.33  
LINK         C   TRP D 196                 N   TPO D 197     1555   1555  1.33  
LINK         C   TPO D 197                 N   LEU D 198     1555   1555  1.44  
LINK         C   VAL D 337                 N   SEP D 338     1555   1555  1.33  
LINK         C   SEP D 338                 N   ILE D 339     1555   1555  1.33  
LINK         OD1 ASP B 184                MG    MG B 351     1555   1555  1.73  
LINK        MG    MG B 352                 O2A ANP B 354     1555   1555  1.88  
LINK         OD2 ASP B 184                MG    MG B 352     1555   1555  1.95  
LINK        MG    MG B 351                 O1B ANP B 354     1555   1555  2.49  
LINK        MG    MG B 352                 O1B ANP B 354     1555   1555  2.84  
CISPEP   1 GLY D  322    ASP D  323          0        -7.55                     
SITE     1 AC1  3 ASP B 166  ASP B 184  ANP B 354                               
SITE     1 AC2  3 ASN B 171  ASP B 184  ANP B 354                               
SITE     1 AC3  4 GLY B  55  ILE B  73  LEU B  74  ASP B  75                    
SITE     1 AC4 18 GLY B  50  THR B  51  VAL B  57  ALA B  70                    
SITE     2 AC4 18 LYS B  72  MET B 120  GLU B 121  VAL B 123                    
SITE     3 AC4 18 GLU B 127  GLU B 170  ASN B 171  ILE B 173                    
SITE     4 AC4 18 THR B 183  ASP B 184  PHE B 327   MG B 351                    
SITE     5 AC4 18  MG B 352  ARG I  18                                          
CRYST1   92.193   92.193  192.186  90.00  90.00 120.00 P 61          6          
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      0.010847  0.006262  0.000000        0.00000                         
SCALE2      0.000000  0.012525  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005203        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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