GenomeNet

Database: PDB
Entry: 3J4R
LinkDB: 3J4R
Original site: 3J4R 
HEADER    TRANSFERASE                             25-SEP-13   3J4R              
TITLE     PSEUDO-ATOMIC MODEL OF THE AKAP18-PKA COMPLEX IN A LINEAR CONFORMATION
TITLE    2 DERIVED FROM ELECTRON MICROSCOPY                                     
CAVEAT     3J4R    CHAIN B RESIDUES 45-91 AND CHAIN C RESIDUES 48-92 ARE        
CAVEAT   2 3J4R    DISORDERED LINKER REGIONS CONNECTING THE STRUCTURED DOMAINS  
CAVEAT   3 3J4R    IN THE PSEUDO-ATOMIC MODEL AND ARE NOT DEFINED BY MAP        
CAVEAT   4 3J4R    DENSITY.                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: A-KINASE ANCHOR PROTEIN 18;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEE REMARK 999;                                            
COMPND   5 SYNONYM: AKAP18;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY     
COMPND   9 SUBUNIT;                                                             
COMPND  10 CHAIN: B, C;                                                         
COMPND  11 SYNONYM: PROTEIN KINASE, CAMP DEPENDENT REGULATORY, TYPE II ALPHA,   
COMPND  12 ISOFORM CRA_B, CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY
COMPND  13 CHAIN, CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY        
COMPND  14 SUBUNIT;                                                             
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND  18 CHAIN: D, E;                                                         
COMPND  19 SYNONYM: PKA C-ALPHA;                                                
COMPND  20 EC: 2.7.11.11;                                                       
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF-9;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 GENE: PRKAR2A, MCG_16488;                                            
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET15A;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 GENE: PRKACA, PKACA;                                                 
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    A-KINASE ANCHORING PROTEIN, CAMP-DEPENDENT KINASE, RII, PKA           
KEYWDS   2 REGULATORY SUBUNIT II, PHOSPHORYLATION, ANCHORING, INTRINSIC         
KEYWDS   3 DISORDER, TRANSFERASE                                                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.L.REICHOW,T.GONEN                                                   
REVDAT   3   18-JUL-18 3J4R    1       REMARK                                   
REVDAT   2   27-NOV-13 3J4R    1       JRNL                                     
REVDAT   1   13-NOV-13 3J4R    0                                                
JRNL        AUTH   F.D.SMITH,S.L.REICHOW,J.L.ESSELTINE,D.SHI,L.K.LANGEBERG,     
JRNL        AUTH 2 J.D.SCOTT,T.GONEN                                            
JRNL        TITL   INTRINSIC DISORDER WITHIN AN AKAP-PROTEIN KINASE A COMPLEX   
JRNL        TITL 2 GUIDES LOCAL SUBSTRATE PHOSPHORYLATION.                      
JRNL        REF    ELIFE                         V.   2 01319 2013              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   24192038                                                     
JRNL        DOI    10.7554/ELIFE.01319                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.   35.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, FREALIGN, IMAGIC            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2IZX                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION                   
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY DETAILS--THIS    
REMARK   3  DOMAIN WAS LINKED TO THE AKAP18 CENTRAL DOMAIN (PDB 2VFL) USING     
REMARK   3  COOT AND THEY WERE FIT TOGETHER INTO THE EM DENSITY.                
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 4.200                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 35.00                          
REMARK   3   NUMBER OF PARTICLES               : 1000                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: (SINGLE PARTICLE DETAILS: IMAGES WERE PROCESSED IN    
REMARK   3  IMAGIC AND ISAC. 3D RECONSTRUCTION WAS DONE IN IMAGIC AND           
REMARK   3  FREALIGN.) (SINGLE PARTICLE--APPLIED SYMMETRY: C1)                  
REMARK   4                                                                      
REMARK   4 3J4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000160249.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NEGATIVE STAINING                 
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : AKAP18-PKA COMPLEX IN LINEAR      
REMARK 245                                    CONFORMATION; A-KINASE            
REMARK 245                                    ANCHORING PROTEIN 18; A-PROTEIN   
REMARK 245                                    KINASE REGULATORY SUBUNIT II      
REMARK 245                                    ALPHA; A-PROTEIN KINASE           
REMARK 245                                    CATALYTIC SUBUNIT                 
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.01                              
REMARK 245   SAMPLE SUPPORT DETAILS         : 200 MESH COPPER GRID WITH THIN    
REMARK 245                                    CARBON SUPPORT                    
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : 25 MM HEPES, PH 7.4, 200 MM       
REMARK 245                                    NACL, 0.5 MM EDTA, 1 MM DTT       
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : HETERO-PENTAMER COMPOSED OF ONE   
REMARK 245  AKAP18 BOUND TO A DIMER OF THE PKA REGULATORY SUBUNIT II AND TWO    
REMARK 245  COPIES OF THE PKA CATALYTIC SUBUNIT                                 
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 01-MAY-12                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 298.00                         
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI 12                  
REMARK 245   DETECTOR TYPE                     : GENERIC GATAN                  
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 50.00                          
REMARK 245   NOMINAL CS                        : 6.30                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 15.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 52000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : LAB6                           
REMARK 245   ACCELERATION VOLTAGE (KV)         : 120                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ASN A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     CYS A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     VAL A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     LEU A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     ASP A    37                                                      
REMARK 465     LEU A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     PHE A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     ASP A    44                                                      
REMARK 465     ILE A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     CYS A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     LEU A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     ASN A    58                                                      
REMARK 465     VAL A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     ASN A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     LYS A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     SER A    67                                                      
REMARK 465     LYS A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     ASP A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     ASN A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     HIS A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     LYS A    79                                                      
REMARK 465     LYS A    80                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     LYS A    82                                                      
REMARK 465     LYS A    83                                                      
REMARK 465     ALA A    84                                                      
REMARK 465     LYS A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     ASP A    87                                                      
REMARK 465     GLN A   318                                                      
REMARK 465     GLN A   319                                                      
REMARK 465     TYR A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     GLU A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     GLN A   325                                                      
REMARK 465     ASN A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     GLN A   329                                                      
REMARK 465     PRO A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     ASN A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     VAL A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     ALA A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     GLY A   341                                                      
REMARK 465     ASP A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     GLY A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     GLY A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     ASP A   349                                                      
REMARK 465     ASN A   350                                                      
REMARK 465     ASN A   351                                                      
REMARK 465     ARG A   352                                                      
REMARK 465     LYS A   353                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     ASN B   112                                                      
REMARK 465     ASP B   113                                                      
REMARK 465     PRO B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     LEU B   395                                                      
REMARK 465     ASP B   396                                                      
REMARK 465     LEU B   397                                                      
REMARK 465     MET B   398                                                      
REMARK 465     ASP B   399                                                      
REMARK 465     PRO B   400                                                      
REMARK 465     GLY B   401                                                      
REMARK 465     GLN B   402                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     ILE C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     ASN C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     PRO C   114                                                      
REMARK 465     ARG C   115                                                      
REMARK 465     LEU C   395                                                      
REMARK 465     ASP C   396                                                      
REMARK 465     LEU C   397                                                      
REMARK 465     MET C   398                                                      
REMARK 465     ASP C   399                                                      
REMARK 465     PRO C   400                                                      
REMARK 465     GLY C   401                                                      
REMARK 465     GLN C   402                                                      
REMARK 465     MET D     0                                                      
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     LYS D   319                                                      
REMARK 465     GLY D   320                                                      
REMARK 465     PRO D   321                                                      
REMARK 465     GLY D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     THR D   324                                                      
REMARK 465     SER D   325                                                      
REMARK 465     ASN D   326                                                      
REMARK 465     PHE D   327                                                      
REMARK 465     ASP D   328                                                      
REMARK 465     ASP D   329                                                      
REMARK 465     TYR D   330                                                      
REMARK 465     GLU D   331                                                      
REMARK 465     MET E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     LYS E   319                                                      
REMARK 465     GLY E   320                                                      
REMARK 465     PRO E   321                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     THR E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     ASN E   326                                                      
REMARK 465     PHE E   327                                                      
REMARK 465     ASP E   328                                                      
REMARK 465     ASP E   329                                                      
REMARK 465     TYR E   330                                                      
REMARK 465     GLU E   331                                                      
REMARK 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     SER B 310    OG                                                  
REMARK 470     LYS B 311    CG   CD   CE   NZ                                   
REMARK 470     THR B 312    OG1  CG2                                            
REMARK 470     LYS B 313    CG   CD   CE   NZ                                   
REMARK 470     SER B 314    OG                                                  
REMARK 470     ASN B 315    CG   OD1  ND2                                       
REMARK 470     LYS B 316    CG   CD   CE   NZ                                   
REMARK 470     ASN B 317    CG   OD1  ND2                                       
REMARK 470     ASN B 320    CG   OD1  ND2                                       
REMARK 470     SER C 310    OG                                                  
REMARK 470     LYS C 311    CG   CD   CE   NZ                                   
REMARK 470     THR C 312    OG1  CG2                                            
REMARK 470     LYS C 313    CG   CD   CE   NZ                                   
REMARK 470     SER C 314    OG                                                  
REMARK 470     ASN C 315    CG   OD1  ND2                                       
REMARK 470     LYS C 316    CG   CD   CE   NZ                                   
REMARK 470     ASN C 317    CG   OD1  ND2                                       
REMARK 470     ASN C 320    CG   OD1  ND2                                       
REMARK 470     GLN D  42    CG   CD   OE1  NE2                                  
REMARK 470     PHE D  43    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP D  44    CG   OD1  OD2                                       
REMARK 470     ARG D  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D  46    CG1  CG2  CD1                                       
REMARK 470     LYS D  47    CG   CD   CE   NZ                                   
REMARK 470     THR D  48    OG1  CG2                                            
REMARK 470     LEU D  49    CG   CD1  CD2                                       
REMARK 470     THR D  51    OG1  CG2                                            
REMARK 470     SER D  53    OG                                                  
REMARK 470     PHE D  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG D  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D  57    CG1  CG2                                            
REMARK 470     MET D  58    CG   SD   CE                                        
REMARK 470     VAL D  60    CG1  CG2                                            
REMARK 470     LYS D  61    CG   CD   CE   NZ                                   
REMARK 470     LYS D  63    CG   CD   CE   NZ                                   
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     SER D  65    OG                                                  
REMARK 470     MET D  71    CG   SD   CE                                        
REMARK 470     LYS D  72    CG   CD   CE   NZ                                   
REMARK 470     ILE D  73    CG1  CG2  CD1                                       
REMARK 470     LEU D  74    CG   CD1  CD2                                       
REMARK 470     ASP D  75    CG   OD1  OD2                                       
REMARK 470     LYS D  76    CG   CD   CE   NZ                                   
REMARK 470     GLN D  77    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  78    CG   CD   CE   NZ                                   
REMARK 470     VAL D  79    CG1  CG2                                            
REMARK 470     VAL D  80    CG1  CG2                                            
REMARK 470     LYS D  81    CG   CD   CE   NZ                                   
REMARK 470     LEU D  82    CG   CD1  CD2                                       
REMARK 470     LYS D 111    CG   CD   CE   NZ                                   
REMARK 470     ASP D 112    CG   OD1  OD2                                       
REMARK 470     ASN D 113    CG   OD1  ND2                                       
REMARK 470     SER D 114    OG                                                  
REMARK 470     ASN D 115    CG   OD1  ND2                                       
REMARK 470     LEU D 116    CG   CD1  CD2                                       
REMARK 470     TYR D 117    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET D 118    CG   SD   CE                                        
REMARK 470     VAL D 119    CG1  CG2                                            
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 345    CG   CD   CE   NZ                                   
REMARK 470     GLU D 349    CG   CD   OE1  OE2                                  
REMARK 470     GLN E  42    CG   CD   OE1  NE2                                  
REMARK 470     PHE E  43    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP E  44    CG   OD1  OD2                                       
REMARK 470     ARG E  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  46    CG1  CG2  CD1                                       
REMARK 470     LYS E  47    CG   CD   CE   NZ                                   
REMARK 470     THR E  48    OG1  CG2                                            
REMARK 470     LEU E  49    CG   CD1  CD2                                       
REMARK 470     THR E  51    OG1  CG2                                            
REMARK 470     SER E  53    OG                                                  
REMARK 470     PHE E  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL E  57    CG1  CG2                                            
REMARK 470     MET E  58    CG   SD   CE                                        
REMARK 470     VAL E  60    CG1  CG2                                            
REMARK 470     LYS E  61    CG   CD   CE   NZ                                   
REMARK 470     LYS E  63    CG   CD   CE   NZ                                   
REMARK 470     GLU E  64    CG   CD   OE1  OE2                                  
REMARK 470     SER E  65    OG                                                  
REMARK 470     MET E  71    CG   SD   CE                                        
REMARK 470     LYS E  72    CG   CD   CE   NZ                                   
REMARK 470     ILE E  73    CG1  CG2  CD1                                       
REMARK 470     LEU E  74    CG   CD1  CD2                                       
REMARK 470     ASP E  75    CG   OD1  OD2                                       
REMARK 470     LYS E  76    CG   CD   CE   NZ                                   
REMARK 470     GLN E  77    CG   CD   OE1  NE2                                  
REMARK 470     LYS E  78    CG   CD   CE   NZ                                   
REMARK 470     VAL E  79    CG1  CG2                                            
REMARK 470     VAL E  80    CG1  CG2                                            
REMARK 470     LYS E  81    CG   CD   CE   NZ                                   
REMARK 470     LEU E  82    CG   CD1  CD2                                       
REMARK 470     LYS E 111    CG   CD   CE   NZ                                   
REMARK 470     ASP E 112    CG   OD1  OD2                                       
REMARK 470     ASN E 113    CG   OD1  ND2                                       
REMARK 470     SER E 114    OG                                                  
REMARK 470     ASN E 115    CG   OD1  ND2                                       
REMARK 470     LEU E 116    CG   CD1  CD2                                       
REMARK 470     TYR E 117    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET E 118    CG   SD   CE                                        
REMARK 470     VAL E 119    CG1  CG2                                            
REMARK 470     GLU E 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 335    CG1  CG2  CD1                                       
REMARK 470     ARG E 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E 339    CG1  CG2  CD1                                       
REMARK 470     LYS E 345    CG   CD   CE   NZ                                   
REMARK 470     GLU E 349    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    PRO B  87   C   -  N   -  CD  ANGL. DEV. = -20.7 DEGREES          
REMARK 500    LYS B 316   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LYS B 316   N   -  CA  -  C   ANGL. DEV. =  20.6 DEGREES          
REMARK 500    PRO C  87   C   -  N   -  CD  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    LYS C 316   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    LYS C 316   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
REMARK 500    VAL D  80   CB  -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    LYS D  81   N   -  CA  -  CB  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LYS D  81   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASN D 113   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    SER D 114   CB  -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    SER D 114   N   -  CA  -  CB  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    SER D 114   CA  -  C   -  O   ANGL. DEV. =  18.9 DEGREES          
REMARK 500    SER D 114   CA  -  C   -  N   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    ASN D 115   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASN D 115   N   -  CA  -  C   ANGL. DEV. =  23.8 DEGREES          
REMARK 500    LEU D 116   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU D 116   CA  -  C   -  O   ANGL. DEV. =  23.2 DEGREES          
REMARK 500    LEU D 116   CA  -  C   -  N   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    VAL E  80   CB  -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    LYS E  81   N   -  CA  -  CB  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LYS E  81   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASN E 113   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    SER E 114   CB  -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    SER E 114   N   -  CA  -  CB  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    SER E 114   CA  -  C   -  O   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    SER E 114   CA  -  C   -  N   ANGL. DEV. = -21.7 DEGREES          
REMARK 500    ASN E 115   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASN E 115   N   -  CA  -  C   ANGL. DEV. =  23.8 DEGREES          
REMARK 500    LEU E 116   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU E 116   CA  -  C   -  O   ANGL. DEV. =  23.2 DEGREES          
REMARK 500    LEU E 116   CA  -  C   -  N   ANGL. DEV. = -23.6 DEGREES          
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    LYS A 238      -17.74    -48.65                                   
REMARK 500    TYR A 263      -71.95   -147.99                                   
REMARK 500    LEU A 301        5.83     80.50                                   
REMARK 500    GLU B 109      102.42    164.89                                   
REMARK 500    GLU B 110      110.06    -12.93                                   
REMARK 500    LYS B 139      -49.75    -28.61                                   
REMARK 500    ASP B 161       -4.68     83.59                                   
REMARK 500    ASP B 189     -138.82     63.35                                   
REMARK 500    ASP B 282      132.28    -35.82                                   
REMARK 500    SER B 301      143.27   -174.60                                   
REMARK 500    SER B 310       77.08    -55.41                                   
REMARK 500    LYS B 311      -43.74   -130.11                                   
REMARK 500    THR B 312       50.56    -69.57                                   
REMARK 500    SER B 314      -85.97    157.51                                   
REMARK 500    ASN B 315       81.97   -176.66                                   
REMARK 500    LYS B 316       74.23     69.46                                   
REMARK 500    ASN B 317      179.05    135.14                                   
REMARK 500    GLN B 321     -123.80   -157.88                                   
REMARK 500    ASN B 342       56.05   -141.84                                   
REMARK 500    SER B 393      -79.76    -46.31                                   
REMARK 500    GLU C 109      102.41    164.96                                   
REMARK 500    GLU C 110      110.03    -12.86                                   
REMARK 500    LYS C 139      -49.58    -28.89                                   
REMARK 500    ASP C 161       -4.45     83.57                                   
REMARK 500    ASP C 189     -138.76     63.33                                   
REMARK 500    ASP C 282      132.25    -35.66                                   
REMARK 500    SER C 301      143.23   -174.60                                   
REMARK 500    SER C 310       77.03    -55.37                                   
REMARK 500    LYS C 311      -43.72   -130.18                                   
REMARK 500    THR C 312       50.61    -69.64                                   
REMARK 500    SER C 314      -85.91    157.56                                   
REMARK 500    ASN C 315       81.90   -176.61                                   
REMARK 500    LYS C 316       74.30     69.32                                   
REMARK 500    ASN C 317      179.18    135.17                                   
REMARK 500    GLN C 321     -123.80   -157.89                                   
REMARK 500    ASN C 342       56.07   -141.85                                   
REMARK 500    SER C 393      -79.62    -46.36                                   
REMARK 500    THR D  32       62.33   -164.54                                   
REMARK 500    ASN D  36       85.65     11.34                                   
REMARK 500    THR D  37      -75.10    -84.67                                   
REMARK 500    ASP D  44     -111.54    -86.76                                   
REMARK 500    ARG D  45      138.94    172.40                                   
REMARK 500    ILE D  46     -118.88   -126.54                                   
REMARK 500    LYS D  47     -169.66    -67.35                                   
REMARK 500    THR D  48       61.15   -150.30                                   
REMARK 500    THR D  51     -109.67    -99.03                                   
REMARK 500    SER D  53       11.89   -161.90                                   
REMARK 500    LYS D  63      -97.13    -77.99                                   
REMARK 500    VAL D  79     -159.74    -61.92                                   
REMARK 500    VAL D  80      -28.14     71.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     101 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-5756   RELATED DB: EMDB                              
REMARK 900 35 ANGSTROM MAP OF THE AKAP18-PKA COMPLEX IN A LINEAR CONFORMATION   
REMARK 900 RELATED ID: EMD-5755   RELATED DB: EMDB                              
REMARK 900 35 ANGSTROM MAP OF THE AKAP18-PKA COMPLEX IN A BENT CONFORMATION     
REMARK 900 RELATED ID: 3J4Q   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AKAP18 IN THIS ENTRY IS FROM HOMO SAPIENS, BUT THE MODELED SEQUENCE  
REMARK 999 IS FROM RATTUS NORVEGICUS (UNP Q6JP77).                              
DBREF  3J4R B    1   402  UNP    Q8K1M3   Q8K1M3_MOUSE     1    402             
DBREF  3J4R C    1   402  UNP    Q8K1M3   Q8K1M3_MOUSE     1    402             
DBREF  3J4R D    0   350  UNP    P05132   KAPCA_MOUSE      1    351             
DBREF  3J4R E    0   350  UNP    P05132   KAPCA_MOUSE      1    351             
DBREF  3J4R A    1   353  PDB    3J4R     3J4R             1    353             
SEQRES   1 A  353  MET GLU ARG PRO ALA ALA GLY GLU ILE ASP ALA ASN LYS          
SEQRES   2 A  353  CYS ASP HIS LEU SER ARG GLY GLU GLU GLY THR GLY ASP          
SEQRES   3 A  353  LEU GLU THR SER PRO VAL GLY SER LEU ALA ASP LEU PRO          
SEQRES   4 A  353  PHE ALA ALA VAL ASP ILE GLN ASP ASP CYS GLY LEU PRO          
SEQRES   5 A  353  ASP VAL PRO GLN GLY ASN VAL PRO GLN GLY ASN PRO LYS          
SEQRES   6 A  353  ARG SER LYS GLU ASN ARG GLY ASP ARG ASN ASP HIS VAL          
SEQRES   7 A  353  LYS LYS ARG LYS LYS ALA LYS LYS ASP TYR GLN PRO ASN          
SEQRES   8 A  353  TYR PHE LEU SER ILE PRO ILE THR ASN LYS LYS ILE THR          
SEQRES   9 A  353  ALA GLY ILE LYS VAL LEU GLN ASN SER ILE LEU ARG GLN          
SEQRES  10 A  353  ASP ASN ARG LEU THR LYS ALA MET VAL GLY ASP GLY SER          
SEQRES  11 A  353  PHE HIS ILE THR LEU LEU VAL MET GLN LEU LEU ASN GLU          
SEQRES  12 A  353  ASP GLU VAL ASN ILE GLY THR ASP ALA LEU LEU GLU LEU          
SEQRES  13 A  353  LYS PRO PHE VAL GLU GLU ILE LEU GLU GLY LYS HIS LEU          
SEQRES  14 A  353  THR LEU PRO PHE HIS GLY ILE GLY THR PHE GLN GLY GLN          
SEQRES  15 A  353  VAL GLY PHE VAL LYS LEU ALA ASP GLY ASP HIS VAL SER          
SEQRES  16 A  353  ALA LEU LEU GLU ILE ALA GLU THR ALA LYS ARG THR PHE          
SEQRES  17 A  353  GLN GLU LYS GLY ILE LEU ALA GLY GLU SER ARG THR PHE          
SEQRES  18 A  353  LYS PRO HIS LEU THR PHE MET LYS LEU SER LYS ALA PRO          
SEQRES  19 A  353  MET LEU TRP LYS LYS GLY VAL ARG LYS ILE GLU PRO GLY          
SEQRES  20 A  353  LEU TYR GLU GLN PHE ILE ASP HIS ARG PHE GLY GLU GLU          
SEQRES  21 A  353  ILE LEU TYR GLN ILE ASP LEU CYS SER MET LEU LYS LYS          
SEQRES  22 A  353  LYS GLN SER ASN GLY TYR TYR HIS CYS GLU SER SER ILE          
SEQRES  23 A  353  VAL ILE GLY GLU LYS ASP ARG LYS GLU PRO GLU ASP ALA          
SEQRES  24 A  353  GLU LEU VAL ARG LEU SER LYS ARG LEU VAL GLU ASN ALA          
SEQRES  25 A  353  VAL LEU LYS ALA VAL GLN GLN TYR LEU GLU GLU THR GLN          
SEQRES  26 A  353  ASN LYS LYS GLN PRO GLY GLU GLY ASN SER VAL LYS ALA          
SEQRES  27 A  353  GLU GLU GLY ASP ARG ASN GLY ASP GLY SER ASP ASN ASN          
SEQRES  28 A  353  ARG LYS                                                      
SEQRES   1 B  402  MET SER HIS ILE GLN ILE PRO ALA GLY LEU THR GLU LEU          
SEQRES   2 B  402  LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN PRO          
SEQRES   3 B  402  PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR ARG          
SEQRES   4 B  402  LEU ARG GLU ALA ARG ARG GLN GLU SER ASP THR PHE ILE          
SEQRES   5 B  402  VAL SER PRO THR THR PHE HIS THR GLN GLU SER SER ALA          
SEQRES   6 B  402  VAL PRO VAL ILE GLU GLU ASP GLY GLU SER ASP SER ASP          
SEQRES   7 B  402  SER GLU ASP ALA ASP LEU GLU VAL PRO VAL PRO SER LYS          
SEQRES   8 B  402  PHE THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN          
SEQRES   9 B  402  PRO ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL          
SEQRES  10 B  402  HIS PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU          
SEQRES  11 B  402  ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN          
SEQRES  12 B  402  GLU GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS          
SEQRES  13 B  402  ILE VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP          
SEQRES  14 B  402  ASP GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR          
SEQRES  15 B  402  ASP ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL          
SEQRES  16 B  402  GLY GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA          
SEQRES  17 B  402  LEU MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA          
SEQRES  18 B  402  THR SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR          
SEQRES  19 B  402  PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG          
SEQRES  20 B  402  LYS MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE          
SEQRES  21 B  402  LYS SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP          
SEQRES  22 B  402  VAL ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE          
SEQRES  23 B  402  ILE ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE          
SEQRES  24 B  402  GLU SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR          
SEQRES  25 B  402  LYS SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE          
SEQRES  26 B  402  ALA HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA          
SEQRES  27 B  402  LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR ALA          
SEQRES  28 B  402  VAL GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA          
SEQRES  29 B  402  PHE GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS          
SEQRES  30 B  402  ARG ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET          
SEQRES  31 B  402  PHE GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN              
SEQRES   1 C  402  MET SER HIS ILE GLN ILE PRO ALA GLY LEU THR GLU LEU          
SEQRES   2 C  402  LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN PRO          
SEQRES   3 C  402  PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR ARG          
SEQRES   4 C  402  LEU ARG GLU ALA ARG ARG GLN GLU SER ASP THR PHE ILE          
SEQRES   5 C  402  VAL SER PRO THR THR PHE HIS THR GLN GLU SER SER ALA          
SEQRES   6 C  402  VAL PRO VAL ILE GLU GLU ASP GLY GLU SER ASP SER ASP          
SEQRES   7 C  402  SER GLU ASP ALA ASP LEU GLU VAL PRO VAL PRO SER LYS          
SEQRES   8 C  402  PHE THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN          
SEQRES   9 C  402  PRO ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL          
SEQRES  10 C  402  HIS PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU          
SEQRES  11 C  402  ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN          
SEQRES  12 C  402  GLU GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS          
SEQRES  13 C  402  ILE VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP          
SEQRES  14 C  402  ASP GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR          
SEQRES  15 C  402  ASP ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL          
SEQRES  16 C  402  GLY GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA          
SEQRES  17 C  402  LEU MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA          
SEQRES  18 C  402  THR SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR          
SEQRES  19 C  402  PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG          
SEQRES  20 C  402  LYS MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE          
SEQRES  21 C  402  LYS SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP          
SEQRES  22 C  402  VAL ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE          
SEQRES  23 C  402  ILE ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE          
SEQRES  24 C  402  GLU SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR          
SEQRES  25 C  402  LYS SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE          
SEQRES  26 C  402  ALA HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA          
SEQRES  27 C  402  LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR ALA          
SEQRES  28 C  402  VAL GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA          
SEQRES  29 C  402  PHE GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS          
SEQRES  30 C  402  ARG ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET          
SEQRES  31 C  402  PHE GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN              
SEQRES   1 D  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN          
SEQRES   2 D  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 D  351  PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA          
SEQRES   4 D  351  GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR          
SEQRES   5 D  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 D  351  SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 D  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 D  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 D  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 D  351  TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE          
SEQRES  11 D  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 D  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 D  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 D  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 D  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 D  351  THR TRP THR LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 D  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 D  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 D  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 D  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 D  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 D  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 D  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 D  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 D  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 D  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 D  351  SER ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE          
SEQRES   1 E  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN          
SEQRES   2 E  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 E  351  PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA          
SEQRES   4 E  351  GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR          
SEQRES   5 E  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 E  351  SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 E  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 E  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 E  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 E  351  TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE          
SEQRES  11 E  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 E  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 E  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 E  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 E  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 E  351  THR TRP THR LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 E  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 E  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 E  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 E  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 E  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 E  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 E  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 E  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 E  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 E  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 E  351  SER ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE          
HELIX    1   1 ASN A  100  ASP A  118  1                                  19    
HELIX    2   2 ASN A  119  MET A  125  5                                   7    
HELIX    3   3 ASN A  142  GLU A  165  1                                  24    
HELIX    4   4 GLY A  191  GLU A  210  1                                  20    
HELIX    5   5 SER A  231  ALA A  233  5                                   3    
HELIX    6   6 PRO A  234  LYS A  239  1                                   6    
HELIX    7   7 GLU A  245  ILE A  253  5                                   9    
HELIX    8   8 ARG A  303  VAL A  317  1                                  15    
HELIX    9   9 LEU B   10  GLN B   25  1                                  16    
HELIX   10  10 ASP B   28  GLU B   42  1                                  15    
HELIX   11  11 THR B  121  LYS B  133  1                                  13    
HELIX   12  12 ILE B  135  ASN B  140  1                                   6    
HELIX   13  13 ASP B  142  MET B  153  1                                  12    
HELIX   14  14 GLY B  205  MET B  210  5                                   6    
HELIX   15  15 ARG B  232  SER B  256  1                                  25    
HELIX   16  16 VAL B  257  LYS B  261  5                                   5    
HELIX   17  17 GLU B  264  ILE B  275  1                                  12    
HELIX   18  18 GLY B  335  VAL B  340  5                                   6    
HELIX   19  19 VAL B  362  GLY B  370  1                                   9    
HELIX   20  20 PRO B  371  ASN B  379  1                                   9    
HELIX   21  21 HIS B  382  GLY B  392  1                                  11    
HELIX   22  22 LEU C   10  GLN C   25  1                                  16    
HELIX   23  23 ASP C   28  GLU C   42  1                                  15    
HELIX   24  24 THR C  121  LYS C  133  1                                  13    
HELIX   25  25 ILE C  135  ASN C  140  1                                   6    
HELIX   26  26 ASP C  142  MET C  153  1                                  12    
HELIX   27  27 GLY C  205  MET C  210  5                                   6    
HELIX   28  28 ARG C  232  SER C  256  1                                  25    
HELIX   29  29 VAL C  257  LYS C  261  5                                   5    
HELIX   30  30 GLU C  264  ILE C  275  1                                  12    
HELIX   31  31 GLY C  335  VAL C  340  5                                   6    
HELIX   32  32 VAL C  362  GLY C  370  1                                   9    
HELIX   33  33 PRO C  371  ASN C  379  1                                   9    
HELIX   34  34 HIS C  382  GLY C  392  1                                  11    
HELIX   35  35 SER D   14  GLU D   31  1                                  18    
HELIX   36  36 GLN D   39  PHE D   43  5                                   5    
HELIX   37  37 ILE D   85  VAL D   98  1                                  14    
HELIX   38  38 MET D  128  GLY D  136  1                                   9    
HELIX   39  39 SER D  139  LEU D  160  1                                  22    
HELIX   40  40 LYS D  168  GLU D  170  5                                   3    
HELIX   41  41 THR D  201  LEU D  205  5                                   5    
HELIX   42  42 ALA D  206  LEU D  211  1                                   6    
HELIX   43  43 LYS D  217  GLY D  234  1                                  18    
HELIX   44  44 GLN D  242  GLY D  253  1                                  12    
HELIX   45  45 SER D  262  LEU D  273  1                                  12    
HELIX   46  46 VAL D  288  ASN D  293  1                                   6    
HELIX   47  47 HIS D  294  ALA D  298  5                                   5    
HELIX   48  48 ASP D  301  GLN D  307  1                                   7    
HELIX   49  49 LYS D  342  GLU D  346  5                                   5    
HELIX   50  50 SER E   14  GLU E   31  1                                  18    
HELIX   51  51 GLN E   39  PHE E   43  5                                   5    
HELIX   52  52 ILE E   85  VAL E   98  1                                  14    
HELIX   53  53 MET E  128  GLY E  136  1                                   9    
HELIX   54  54 SER E  139  LEU E  160  1                                  22    
HELIX   55  55 LYS E  168  GLU E  170  5                                   3    
HELIX   56  56 THR E  201  LEU E  205  5                                   5    
HELIX   57  57 ALA E  206  LEU E  211  1                                   6    
HELIX   58  58 LYS E  217  GLY E  234  1                                  18    
HELIX   59  59 GLN E  242  GLY E  253  1                                  12    
HELIX   60  60 SER E  262  LEU E  273  1                                  12    
HELIX   61  61 VAL E  288  ASN E  293  1                                   6    
HELIX   62  62 HIS E  294  ALA E  298  5                                   5    
HELIX   63  63 ASP E  301  GLN E  307  1                                   7    
HELIX   64  64 LYS E  342  GLU E  346  5                                   5    
SHEET    1   A 4 HIS A 132  MET A 138  0                                        
SHEET    2   A 4 TYR A  92  PRO A  97 -1  N  LEU A  94   O  LEU A 135           
SHEET    3   A 4 GLN A 264  SER A 269 -1  O  CYS A 268   N  PHE A  93           
SHEET    4   A 4 HIS A 281  VAL A 287 -1  O  SER A 284   N  LEU A 267           
SHEET    1   B 4 HIS A 224  LYS A 229  0                                        
SHEET    2   B 4 VAL A 183  LEU A 188 -1  N  GLY A 184   O  PHE A 227           
SHEET    3   B 4 THR A 170  PHE A 179 -1  N  GLY A 177   O  PHE A 185           
SHEET    4   B 4 ARG A 256  ILE A 261 -1  O  GLU A 260   N  LEU A 171           
SHEET    1   C 2 VAL B  98  CYS B  99  0                                        
SHEET    2   C 2 CYS D 199  GLY D 200 -1  O  GLY D 200   N  VAL B  98           
SHEET    1   D 4 PHE B 154  VAL B 158  0                                        
SHEET    2   D 4 GLY B 225  ASP B 231 -1  O  GLY B 229   N  PHE B 154           
SHEET    3   D 4 ASN B 173  ARG B 179 -1  N  VAL B 176   O  TRP B 228           
SHEET    4   D 4 SER B 203  PHE B 204 -1  O  PHE B 204   N  TYR B 175           
SHEET    1   E 4 HIS B 163  ILE B 165  0                                        
SHEET    2   E 4 THR B 218  ALA B 221 -1  O  ILE B 219   N  VAL B 164           
SHEET    3   E 4 THR B 181  LYS B 188 -1  N  LEU B 185   O  THR B 218           
SHEET    4   E 4 GLN B 191  ASP B 199 -1  O  GLY B 196   N  ILE B 184           
SHEET    1   F 4 GLY B 276  TYR B 280  0                                        
SHEET    2   F 4 SER B 348  ASP B 361 -1  O  VAL B 355   N  TYR B 280           
SHEET    3   F 4 SER B 295  ILE B 308 -1  N  GLU B 303   O  VAL B 352           
SHEET    4   F 4 VAL B 323  HIS B 329 -1  O  VAL B 323   N  ILE B 308           
SHEET    1   G 4 ARG B 285  ILE B 287  0                                        
SHEET    2   G 4 SER B 348  ASP B 361 -1  O  ALA B 349   N  ILE B 286           
SHEET    3   G 4 SER B 295  ILE B 308 -1  N  GLU B 303   O  VAL B 352           
SHEET    4   G 4 TYR B 333  PHE B 334 -1  O  PHE B 334   N  TYR B 297           
SHEET    1   H 2 VAL C  98  CYS C  99  0                                        
SHEET    2   H 2 CYS E 199  GLY E 200 -1  O  GLY E 200   N  VAL C  98           
SHEET    1   I 4 PHE C 154  VAL C 158  0                                        
SHEET    2   I 4 GLY C 225  ASP C 231 -1  O  GLY C 229   N  PHE C 154           
SHEET    3   I 4 ASN C 173  ARG C 179 -1  N  VAL C 176   O  TRP C 228           
SHEET    4   I 4 SER C 203  PHE C 204 -1  O  PHE C 204   N  TYR C 175           
SHEET    1   J 4 HIS C 163  ILE C 165  0                                        
SHEET    2   J 4 THR C 218  ALA C 221 -1  O  ILE C 219   N  VAL C 164           
SHEET    3   J 4 THR C 181  LYS C 188 -1  N  LEU C 185   O  THR C 218           
SHEET    4   J 4 GLN C 191  ASP C 199 -1  O  GLY C 196   N  ILE C 184           
SHEET    1   K 4 GLY C 276  TYR C 280  0                                        
SHEET    2   K 4 SER C 348  ASP C 361 -1  O  VAL C 355   N  TYR C 280           
SHEET    3   K 4 SER C 295  ILE C 308 -1  N  GLU C 303   O  VAL C 352           
SHEET    4   K 4 VAL C 323  HIS C 329 -1  O  VAL C 323   N  ILE C 308           
SHEET    1   L 4 ARG C 285  ILE C 287  0                                        
SHEET    2   L 4 SER C 348  ASP C 361 -1  O  ALA C 349   N  ILE C 286           
SHEET    3   L 4 SER C 295  ILE C 308 -1  N  GLU C 303   O  VAL C 352           
SHEET    4   L 4 TYR C 333  PHE C 334 -1  O  PHE C 334   N  TYR C 297           
SHEET    1   M 4 ARG D  56  LYS D  61  0                                        
SHEET    2   M 4 HIS D  68  ILE D  73 -1  O  TYR D  69   N  VAL D  60           
SHEET    3   M 4 TYR D 117  GLU D 121 -1  O  MET D 120   N  ALA D  70           
SHEET    4   M 4 LEU D 106  PHE D 110 -1  N  PHE D 108   O  VAL D 119           
SHEET    1   N 3 GLY D 126  GLU D 127  0                                        
SHEET    2   N 3 LEU D 172  ILE D 174 -1  O  ILE D 174   N  GLY D 126           
SHEET    3   N 3 ILE D 180  VAL D 182 -1  O  GLN D 181   N  LEU D 173           
SHEET    1   O 2 LEU D 162  ILE D 163  0                                        
SHEET    2   O 2 LYS D 189  ARG D 190 -1  O  LYS D 189   N  ILE D 163           
SHEET    1   P 4 ARG E  56  LYS E  61  0                                        
SHEET    2   P 4 HIS E  68  ILE E  73 -1  O  TYR E  69   N  VAL E  60           
SHEET    3   P 4 TYR E 117  GLU E 121 -1  O  MET E 120   N  ALA E  70           
SHEET    4   P 4 LEU E 106  PHE E 110 -1  N  PHE E 108   O  VAL E 119           
SHEET    1   Q 3 GLY E 126  GLU E 127  0                                        
SHEET    2   Q 3 LEU E 172  ILE E 174 -1  O  ILE E 174   N  GLY E 126           
SHEET    3   Q 3 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
SHEET    1   R 2 LEU E 162  ILE E 163  0                                        
SHEET    2   R 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
CISPEP   1 GLU A  290    LYS A  291          0        13.02                     
CISPEP   2 LYS A  291    ASP A  292          0        -7.14                     
CISPEP   3 ALA A  299    GLU A  300          0         0.08                     
CISPEP   4 ARG B   44    ARG B   45          0        -4.14                     
CISPEP   5 SER B   54    PRO B   55          0       -14.62                     
CISPEP   6 PRO B   89    SER B   90          0        -1.49                     
CISPEP   7 PHE B   92    THR B   93          0         0.90                     
CISPEP   8 VAL C   86    PRO C   87          0         8.08                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system