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Database: PDB
Entry: 4DC2
LinkDB: 4DC2
Original site: 4DC2 
HEADER    TRANSFERASE/TRANSFERASE SUBSTRATE       17-JAN-12   4DC2              
TITLE     STRUCTURE OF PKC IN COMPLEX WITH A SUBSTRATE PEPTIDE FROM PAR-3       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE C IOTA TYPE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 231-595;                                      
COMPND   5 SYNONYM: PKC, ATYPICAL PROTEIN KINASE C-LAMBDA/IOTA, APKC-           
COMPND   6 LAMBDA/IOTA, NPKC-IOTA;                                              
COMPND   7 EC: 2.7.11.13;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PARTITIONING DEFECTIVE 3 HOMOLOG;                          
COMPND  11 CHAIN: Z;                                                            
COMPND  12 FRAGMENT: SUBSTRATE PEPTIDE, UNP RESIDUES 813-840;                   
COMPND  13 SYNONYM: PAR-3, PARD-3, ATYPICAL PKC ISOTYPE-SPECIFIC-INTERACTING    
COMPND  14 PROTEIN, ASIP, ATYPICAL PKC-SPECIFIC-BINDING PROTEIN, ASBP;          
COMPND  15 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: PKCL;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: RAT;                                                
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS/MOUSES/RATS. 
KEYWDS    KINASE, SUBSTRATE, CELL POLARITY, PAR-3, ATYPICAL PKC, TRANSFERASE-   
KEYWDS   2 TRANSFERASE SUBSTRATE COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHANG,C.WANG,J.YU,M.ZHANG                                           
REVDAT   1   11-JUL-12 4DC2    0                                                
JRNL        AUTH   C.WANG,Y.SHANG,J.YU,M.ZHANG                                  
JRNL        TITL   SUBSTRATE RECOGNITION MECHANISM OF ATYPICAL PROTEIN KINASE   
JRNL        TITL 2 CS REVEALED BY THE STRUCTURE OF PKC IOTA IN COMPLEX WITH A   
JRNL        TITL 3 SUBSTRATE PEPTIDE FROM PAR-3                                 
JRNL        REF    STRUCTURE                     V.  20   791 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22579248                                                     
JRNL        DOI    10.1016/J.STR.2012.02.022                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_629)                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13400                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 659                             
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 21.1803 -  4.0961    0.83     2613   149  0.1556 0.1973        
REMARK   3     2  4.0961 -  3.2550    0.86     2651   130  0.1556 0.2488        
REMARK   3     3  3.2550 -  2.8446    0.86     2647   132  0.1904 0.2723        
REMARK   3     4  2.8446 -  2.5850    0.82     2509   129  0.2048 0.2982        
REMARK   3     5  2.5850 -  2.4000    0.76     2321   119  0.2136 0.2990        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 45.25                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.250           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.16920                                             
REMARK   3    B22 (A**2) : 0.69700                                              
REMARK   3    B33 (A**2) : 1.47220                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 1.22380                                              
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      :  0.008           2764                                  
REMARK   3   ANGLE     :  1.132           3747                                  
REMARK   3   CHIRALITY :  0.078            406                                  
REMARK   3   PLANARITY :  0.005            485                                  
REMARK   3   DIHEDRAL  : 14.204            981                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 239:394)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5796  -9.7113  13.7984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1875 T22:   0.1802                                     
REMARK   3      T33:   0.1293 T12:  -0.0466                                     
REMARK   3      T13:   0.0348 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5296 L22:   0.5216                                     
REMARK   3      L33:   0.7620 L12:   0.3886                                     
REMARK   3      L13:   0.4306 L23:  -0.0453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1334 S12:   0.2568 S13:  -0.0035                       
REMARK   3      S21:  -0.1277 S22:   0.1525 S23:  -0.0873                       
REMARK   3      S31:  -0.1956 S32:   0.0688 S33:  -0.0355                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 395:469)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4416 -25.6088  27.4723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0993 T22:   0.0395                                     
REMARK   3      T33:   0.1509 T12:   0.0122                                     
REMARK   3      T13:  -0.0555 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2494 L22:   0.0624                                     
REMARK   3      L33:   0.5965 L12:   0.0105                                     
REMARK   3      L13:   0.0467 L23:  -0.1317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0090 S12:  -0.0222 S13:  -0.1627                       
REMARK   3      S21:   0.0665 S22:   0.0475 S23:  -0.1527                       
REMARK   3      S31:   0.2727 S32:  -0.1993 S33:  -0.0473                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 470:577)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0215 -12.8381  19.0586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0402 T22:  -0.1354                                     
REMARK   3      T33:  -0.0795 T12:  -0.1655                                     
REMARK   3      T13:  -0.0554 T23:  -0.2453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2585 L22:   0.3641                                     
REMARK   3      L33:   0.6701 L12:   0.0337                                     
REMARK   3      L13:   0.0979 L23:   0.0581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:  -0.0014 S13:  -0.0101                       
REMARK   3      S21:   0.0130 S22:   0.4192 S23:   0.1662                       
REMARK   3      S31:  -0.4131 S32:  -0.5495 S33:   0.0641                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain Z and resid 1047:1062)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9009 -15.1037  31.7255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1578 T22:   0.2544                                     
REMARK   3      T33:   0.3517 T12:  -0.0511                                     
REMARK   3      T13:   0.0253 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2002 L22:   0.6255                                     
REMARK   3      L33:   0.0855 L12:  -0.0206                                     
REMARK   3      L13:   0.1039 L23:   0.0760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0954 S12:   0.0209 S13:  -0.0974                       
REMARK   3      S21:   0.0909 S22:   0.0117 S23:  -0.2522                       
REMARK   3      S31:   0.1370 S32:   0.0877 S33:  -0.0024                       
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 4DC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070141.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13400                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, PH 7.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.72800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.72800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.45000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Z                                  
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   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     TYR A   193                                                      
REMARK 465     TYR A   194                                                      
REMARK 465     HIS A   195                                                      
REMARK 465     HIS A   196                                                      
REMARK 465     HIS A   197                                                      
REMARK 465     HIS A   198                                                      
REMARK 465     HIS A   199                                                      
REMARK 465     HIS A   200                                                      
REMARK 465     ASP A   201                                                      
REMARK 465     TYR A   202                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     ILE A   204                                                      
REMARK 465     PRO A   205                                                      
REMARK 465     THR A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     ASN A   209                                                      
REMARK 465     LEU A   210                                                      
REMARK 465     TYR A   211                                                      
REMARK 465     PHE A   212                                                      
REMARK 465     GLN A   213                                                      
REMARK 465     GLY A   214                                                      
REMARK 465     ALA A   215                                                      
REMARK 465     MET A   216                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     SER A   218                                                      
REMARK 465     GLY A   219                                                      
REMARK 465     ILE A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     GLU A   223                                                      
REMARK 465     LYS A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     MET A   227                                                      
REMARK 465     ASN A   228                                                      
REMARK 465     THR A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     SER A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     ASP A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     ASP A   285                                                      
REMARK 465     SER A   449                                                      
REMARK 465     ASP A   450                                                      
REMARK 465     ASN A   451                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     ASP A   453                                                      
REMARK 465     GLN A   454                                                      
REMARK 465     LEU A   578                                                      
REMARK 465     LEU A   579                                                      
REMARK 465     MET A   580                                                      
REMARK 465     SER A   581                                                      
REMARK 465     ALA A   582                                                      
REMARK 465     GLU A   583                                                      
REMARK 465     GLU A   584                                                      
REMARK 465     CYS A   585                                                      
REMARK 465     VAL A   586                                                      
REMARK 465     ASP Z  1046                                                      
REMARK 465     GLU Z  1063                                                      
REMARK 465     LYS Z  1064                                                      
REMARK 465     ARG Z  1065                                                      
REMARK 465     THR Z  1066                                                      
REMARK 465     LYS Z  1067                                                      
REMARK 465     GLN Z  1068                                                      
REMARK 465     PHE Z  1069                                                      
REMARK 465     SER Z  1070                                                      
REMARK 465     ASN Z  1071                                                      
REMARK 465     ALA Z  1072                                                      
REMARK 465     SER Z  1073                                                      
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     ARG A 248    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 252    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     ARG A 268    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 278    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 281    CG   OD1  ND2                                       
REMARK 470     ILE A 286    CG1  CG2  CD1                                       
REMARK 470     GLN A 290    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 315    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 395    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 455    CG   OD1  ND2                                       
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 470    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 492    CG   CD   CE   NZ                                   
REMARK 470     GLU A 493    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 513    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 536    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 553    CG   CD1  CD2                                       
REMARK 470     ASP A 556    CG   OD1  OD2                                       
REMARK 470     ASP A 557    CG   OD1  OD2                                       
REMARK 470     ASP A 558    CG   OD1  OD2                                       
REMARK 470     ASP A 559    CG   OD1  OD2                                       
REMARK 470     ILE A 560    CG1  CG2  CD1                                       
REMARK 470     ARG A 562    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 563    CG   CD   CE   NZ                                   
REMARK 470     ILE A 564    CG1  CG2  CD1                                       
REMARK 470     ASP A 565    CG   OD1  OD2                                       
REMARK 470     GLU A 568    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 570    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z1054    CG   CD   OE1  OE2                                  
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     SER A  476   CA   CB   OG                                        
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    GLU A 278        0.16    -57.33                                   
REMARK 500    THR A 314     -167.98   -104.46                                   
REMARK 500    ARG A 338      -51.40     68.25                                   
REMARK 500    ARG A 367       -5.86     70.59                                   
REMARK 500    ASP A 386       97.17     60.87                                   
REMARK 500    PHE A 537       -7.89     91.12                                   
REMARK 500    GLN A 545       -7.50    -58.62                                   
REMARK 500    LYS A 563       36.11    -98.01                                   
REMARK 500    GLU A 568        2.84    -68.87                                   
REMARK 500    LEU Z1049       48.05    -96.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 744        DISTANCE =  5.08 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE A 601                 
DBREF  4DC2 A  222   586  UNP    Q62074   KPCI_MOUSE     231    595             
DBREF  4DC2 Z 1046  1073  UNP    Q9Z340   PARD3_RAT      813    840             
SEQADV 4DC2 MET A  191  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 SER A  192  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 TYR A  193  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 TYR A  194  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  195  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  196  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  197  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  198  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  199  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 HIS A  200  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ASP A  201  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 TYR A  202  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ASP A  203  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ILE A  204  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 PRO A  205  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 THR A  206  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 THR A  207  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLU A  208  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ASN A  209  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 LEU A  210  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 TYR A  211  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 PHE A  212  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLN A  213  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLY A  214  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ALA A  215  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 MET A  216  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLY A  217  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 SER A  218  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLY A  219  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ILE A  220  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 GLU A  221  UNP  Q62074              EXPRESSION TAG                 
SEQADV 4DC2 ARG A  273  UNP  Q62074    LYS   282 CONFLICT                       
SEQRES   1 A  396  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  396  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A  396  GLY SER GLY ILE GLU GLU GLU LYS GLU ALA MET ASN THR          
SEQRES   4 A  396  ARG GLU SER GLY LYS ALA SER SER SER LEU GLY LEU GLN          
SEQRES   5 A  396  ASP PHE ASP LEU LEU ARG VAL ILE GLY ARG GLY SER TYR          
SEQRES   6 A  396  ALA LYS VAL LEU LEU VAL ARG LEU LYS LYS THR ASP ARG          
SEQRES   7 A  396  ILE TYR ALA MET ARG VAL VAL LYS LYS GLU LEU VAL ASN          
SEQRES   8 A  396  ASP ASP GLU ASP ILE ASP TRP VAL GLN THR GLU LYS HIS          
SEQRES   9 A  396  VAL PHE GLU GLN ALA SER ASN HIS PRO PHE LEU VAL GLY          
SEQRES  10 A  396  LEU HIS SER CYS PHE GLN THR GLU SER ARG LEU PHE PHE          
SEQRES  11 A  396  VAL ILE GLU TYR VAL ASN GLY GLY ASP LEU MET PHE HIS          
SEQRES  12 A  396  MET GLN ARG GLN ARG LYS LEU PRO GLU GLU HIS ALA ARG          
SEQRES  13 A  396  PHE TYR SER ALA GLU ILE SER LEU ALA LEU ASN TYR LEU          
SEQRES  14 A  396  HIS GLU ARG GLY ILE ILE TYR ARG ASP LEU LYS LEU ASP          
SEQRES  15 A  396  ASN VAL LEU LEU ASP SER GLU GLY HIS ILE LYS LEU THR          
SEQRES  16 A  396  ASP TYR GLY MET CYS LYS GLU GLY LEU ARG PRO GLY ASP          
SEQRES  17 A  396  THR THR SER THR PHE CYS GLY THR PRO ASN TYR ILE ALA          
SEQRES  18 A  396  PRO GLU ILE LEU ARG GLY GLU ASP TYR GLY PHE SER VAL          
SEQRES  19 A  396  ASP TRP TRP ALA LEU GLY VAL LEU MET PHE GLU MET MET          
SEQRES  20 A  396  ALA GLY ARG SER PRO PHE ASP ILE VAL GLY SER SER ASP          
SEQRES  21 A  396  ASN PRO ASP GLN ASN THR GLU ASP TYR LEU PHE GLN VAL          
SEQRES  22 A  396  ILE LEU GLU LYS GLN ILE ARG ILE PRO ARG SER LEU SER          
SEQRES  23 A  396  VAL LYS ALA ALA SER VAL LEU LYS SER PHE LEU ASN LYS          
SEQRES  24 A  396  ASP PRO LYS GLU ARG LEU GLY CYS HIS PRO GLN THR GLY          
SEQRES  25 A  396  PHE ALA ASP ILE GLN GLY HIS PRO PHE PHE ARG ASN VAL          
SEQRES  26 A  396  ASP TRP ASP MET MET GLU GLN LYS GLN VAL VAL PRO PRO          
SEQRES  27 A  396  PHE LYS PRO ASN ILE SER GLY GLU PHE GLY LEU ASP ASN          
SEQRES  28 A  396  PHE ASP SER GLN PHE THR ASN GLU PRO VAL GLN LEU TPO          
SEQRES  29 A  396  PRO ASP ASP ASP ASP ILE VAL ARG LYS ILE ASP GLN SER          
SEQRES  30 A  396  GLU PHE GLU GLY PHE GLU TYR ILE ASN PRO LEU LEU MET          
SEQRES  31 A  396  SER ALA GLU GLU CYS VAL                                      
SEQRES   1 Z   28  ASP PRO VAL LEU ALA PHE GLN ARG GLU GLY PHE GLY ARG          
SEQRES   2 Z   28  GLN SER MET SER GLU LYS ARG THR LYS GLN PHE SER ASN          
SEQRES   3 Z   28  ALA SER                                                      
MODRES 4DC2 TPO A  554  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 554      11                                                       
HET    ADE  A 601      10                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADE ADENINE                                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  ADE    C5 H5 N5                                                     
FORMUL   4  HOH   *52(H2 O)                                                     
HELIX    1   1 GLY A  240  GLN A  242  5                                   3    
HELIX    2   2 GLU A  278  VAL A  280  5                                   3    
HELIX    3   3 ASP A  287  SER A  300  1                                  14    
HELIX    4   4 ASP A  329  ARG A  338  1                                  10    
HELIX    5   5 PRO A  341  ARG A  362  1                                  22    
HELIX    6   6 LYS A  370  ASP A  372  5                                   3    
HELIX    7   7 THR A  406  ILE A  410  5                                   5    
HELIX    8   8 ALA A  411  ARG A  416  1                                   6    
HELIX    9   9 PHE A  422  GLY A  439  1                                  18    
HELIX   10  10 THR A  456  LYS A  467  1                                  12    
HELIX   11  11 SER A  476  LEU A  487  1                                  12    
HELIX   12  12 THR A  501  HIS A  509  1                                   9    
HELIX   13  13 ASP A  516  GLN A  522  1                                   7    
HELIX   14  14 GLY A  538  PHE A  542  5                                   5    
HELIX   15  15 ASP A  543  ASN A  548  1                                   6    
HELIX   16  16 ASP A  557  ARG A  562  1                                   6    
HELIX   17  17 ASP A  565  GLU A  570  5                                   6    
SHEET    1   A 6 PHE A 244  ARG A 252  0                                        
SHEET    2   A 6 ALA A 256  LEU A 263 -1  O  LEU A 260   N  ARG A 248           
SHEET    3   A 6 ILE A 269  LYS A 276 -1  O  TYR A 270   N  VAL A 261           
SHEET    4   A 6 ARG A 317  GLU A 323 -1  O  LEU A 318   N  VAL A 275           
SHEET    5   A 6 LEU A 308  GLN A 313 -1  N  HIS A 309   O  VAL A 321           
SHEET    6   A 6 TYR A 574  ILE A 575 -1  O  TYR A 574   N  CYS A 311           
SHEET    1   B 2 VAL A 374  LEU A 376  0                                        
SHEET    2   B 2 ILE A 382  LEU A 384 -1  O  LYS A 383   N  LEU A 375           
LINK         C   LEU A 553                 N   TPO A 554     1555   1555  1.33  
LINK         C   TPO A 554                 N   PRO A 555     1555   1555  1.34  
SITE     1 AC1  6 ILE A 322  GLU A 323  VAL A 325  LEU A 375                    
SITE     2 AC1  6 THR A 385  PHE A 542                                          
CRYST1  101.456   54.900   82.489  90.00 115.18  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009856  0.000000  0.004633        0.00000                         
SCALE2      0.000000  0.018215  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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