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Database: PDB
Entry: 2MKJ
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Original site: 2MKJ 
HEADER    TRANSLATION REGULATOR                   07-FEB-14   2MKJ              
TITLE     SOLUTION STRUCTURE OF TANDEM RRM DOMAINS OF CYTOPLASMIC               
TITLE    2 POLYADENYLATION ELEMENT BINDING PROTEIN 4 (CPEB4) IN FREE STATE      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOPLASMIC POLYADENYLATION ELEMENT-BINDING PROTEIN 4;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 53-254;                                       
COMPND   5 SYNONYM: CPE-BP4, CPE-BINDING PROTEIN 4, HCPEB-4;                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CPEB4, KIAA1673;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28A(+)                                  
KEYWDS    CPEB4, RNA RECOGNITION MOTIF (RRM), CYTOPLASMIC POLYADENYLATION,      
KEYWDS   2 TRANSLATIONAL REGULATION, TRANSLATION REGULATOR                      
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    T.AFROZ,L.SKRISOVSKA,E.BELLOC,J.G.BOIXET,R.MENDEZ,F.H.-T.ALLAIN       
REVDAT   3   14-JUN-23 2MKJ    1       REMARK                                   
REVDAT   2   27-APR-16 2MKJ    1       DBREF  SEQRES                            
REVDAT   1   23-JUL-14 2MKJ    0                                                
JRNL        AUTH   T.AFROZ,L.SKRISOVSKA,E.BELLOC,J.GUILLEN-BOIXET,R.MENDEZ,     
JRNL        AUTH 2 F.H.-T.ALLAIN                                                
JRNL        TITL   A FLY TRAP MECHANISM PROVIDES SEQUENCE-SPECIFIC RNA          
JRNL        TITL 2 RECOGNITION BY CPEB PROTEINS                                 
JRNL        REF    GENES DEV.                    V.  28  1498 2014              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   24990967                                                     
JRNL        DOI    10.1101/GAD.241133.114                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER                                                
REMARK   3   AUTHORS     : CASE, DARDEN, CHEATHAM, III, SIMMERLING, WANG,       
REMARK   3                 DUKE, LUO, ... AND KOLLMAN                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2MKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000103724.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 0.15                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.4-0.6 MM [U-100% 13C; U-100%     
REMARK 210                                   15N] CPEB4RRM12-1, 100 MM SODIUM   
REMARK 210                                   CHLORIDE-2, 50 MM SODIUM           
REMARK 210                                   PHOSPHATE-3, 1 MM DTT-4, 90% H2O/  
REMARK 210                                   10% D2O; 0.4-0.6 MM [U-100% 13C;   
REMARK 210                                   U-100% 15N; U-80% 2H] CPEB4RRM12-  
REMARK 210                                   5, 100 MM SODIUM CHLORIDE-6, 50    
REMARK 210                                   MM SODIUM PHOSPHATE-7, 1 MM DTT-   
REMARK 210                                   8, 90% H2O/10% D2O; 0.4-0.6 MM     
REMARK 210                                   [U-100% 15N] CPEB4RRM12-9, 100     
REMARK 210                                   MM SODIUM CHLORIDE-10, 50 MM       
REMARK 210                                   SODIUM PHOSPHATE-11, 1 MM DTT-12,  
REMARK 210                                   90% H2O/10% D2O; 0.4-0.6 MM [U-    
REMARK 210                                   100% 15N] CPEB4RRM12-13, 100 MM    
REMARK 210                                   SODIUM CHLORIDE-14, 50 MM SODIUM   
REMARK 210                                   PHOSPHATE-15, 1 MM DTT-16, 100%    
REMARK 210                                   D2O                                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 2D TROSY; 2D 1H    
REMARK 210                                   -13C HSQC; 2D 1H-13C HSQC          
REMARK 210                                   ALIPHATIC; 2D 1H-13C HSQC          
REMARK 210                                   AROMATIC; 2D 1H-1H TOCSY; 2D 1H-   
REMARK 210                                   1H NOESY; 3D CBCA(CO)NH; 3D        
REMARK 210                                   TRHNCACB; 3D TRHN(CO)CA; 3D        
REMARK 210                                   TRHNCO; 3D TRHCACO; 3D HCCH-       
REMARK 210                                   TOCSY; 3D 1H-15N NOESY; 3D 1H-     
REMARK 210                                   13C NOESY ALIPHATIC; 3D 1H-13C     
REMARK 210                                   NOESY AROMATIC                     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ; 700 MHZ; 600 MHZ; 500     
REMARK 210                                   MHZ                                
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA, SPARKY, TOPSPIN             
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 30                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     LEU A   255                                                      
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  1 GLN A  55      -32.64   -151.84                                   
REMARK 500  1 ARG A  87      -17.22     60.65                                   
REMARK 500  1 LYS A  98       12.19   -156.20                                   
REMARK 500  1 LYS A 102      -54.24   -151.11                                   
REMARK 500  1 CYS A 138       39.70    -90.77                                   
REMARK 500  1 SER A 140      109.55    -54.17                                   
REMARK 500  1 SER A 141      -44.88   -167.25                                   
REMARK 500  1 PRO A 142     -145.75    -75.08                                   
REMARK 500  1 THR A 143        9.95    -66.11                                   
REMARK 500  1 ASP A 146       12.57     54.20                                   
REMARK 500  1 SER A 159       -3.18    -50.17                                   
REMARK 500  1 MET A 163      -30.29   -134.87                                   
REMARK 500  1 ALA A 186       13.24    -69.85                                   
REMARK 500  1 TYR A 197       42.28   -140.91                                   
REMARK 500  1 ALA A 217     -165.06    -55.95                                   
REMARK 500  1 SER A 223       26.00   -148.92                                   
REMARK 500  1 ASP A 245      -32.27   -131.51                                   
REMARK 500  2 ARG A  59      172.18     60.56                                   
REMARK 500  2 PRO A  73      155.71    -49.82                                   
REMARK 500  2 ARG A  87       -1.81   -141.84                                   
REMARK 500  2 PRO A  90       10.31    -64.95                                   
REMARK 500  2 LYS A  98       11.87   -144.48                                   
REMARK 500  2 LYS A 108       13.16     51.91                                   
REMARK 500  2 PRO A 142       -5.05    -54.85                                   
REMARK 500  2 ILE A 144      -25.47   -143.28                                   
REMARK 500  2 LYS A 147      161.36     62.04                                   
REMARK 500  2 LEU A 156        6.88    -69.73                                   
REMARK 500  2 SER A 159      -18.26    -43.82                                   
REMARK 500  2 MET A 163       -0.19   -140.02                                   
REMARK 500  2 ASP A 164      169.62     59.54                                   
REMARK 500  2 ARG A 185       46.80    -93.82                                   
REMARK 500  2 LEU A 196      -72.88   -103.77                                   
REMARK 500  2 CYS A 201      -50.93   -153.37                                   
REMARK 500  2 ALA A 217      176.48     59.39                                   
REMARK 500  2 PHE A 222       28.35   -158.90                                   
REMARK 500  2 ASN A 224       -3.53   -147.51                                   
REMARK 500  2 GLN A 238      -77.76    -84.20                                   
REMARK 500  2 LEU A 239      163.81     59.62                                   
REMARK 500  2 ARG A 247      117.60     56.01                                   
REMARK 500  3 ARG A  59       18.49     56.03                                   
REMARK 500  3 PHE A  85       63.90   -106.29                                   
REMARK 500  3 ARG A  86        1.55    -68.93                                   
REMARK 500  3 SER A 103      165.96     56.39                                   
REMARK 500  3 TYR A 104       15.12   -142.64                                   
REMARK 500  3 LYS A 108       18.54   -155.29                                   
REMARK 500  3 SER A 141      -45.95   -158.02                                   
REMARK 500  3 ASP A 146      -92.82   -151.87                                   
REMARK 500  3 ASN A 155       56.50    -91.34                                   
REMARK 500  3 PRO A 181      176.87    -57.03                                   
REMARK 500  3 ALA A 186        8.96    -68.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     371 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 19777   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 2MKE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2MKH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2MKI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2MKK   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS PROTEIN SEQUENCE IS ISOFORM 3 OF CPEB4_HUMAN.                   
DBREF  2MKJ A   53   255  UNP    Q17RY0   CPEB4_HUMAN     53    255             
SEQRES   1 A  203  SER HIS GLN ASN GLY GLU ARG VAL GLU ARG TYR SER ARG          
SEQRES   2 A  203  LYS VAL PHE VAL GLY GLY LEU PRO PRO ASP ILE ASP GLU          
SEQRES   3 A  203  ASP GLU ILE THR ALA SER PHE ARG ARG PHE GLY PRO LEU          
SEQRES   4 A  203  ILE VAL ASP TRP PRO HIS LYS ALA GLU SER LYS SER TYR          
SEQRES   5 A  203  PHE PRO PRO LYS GLY TYR ALA PHE LEU LEU PHE GLN ASP          
SEQRES   6 A  203  GLU SER SER VAL GLN ALA LEU ILE ASP ALA CYS ILE GLU          
SEQRES   7 A  203  GLU ASP GLY LYS LEU TYR LEU CYS VAL SER SER PRO THR          
SEQRES   8 A  203  ILE LYS ASP LYS PRO VAL GLN ILE ARG PRO TRP ASN LEU          
SEQRES   9 A  203  SER ASP SER ASP PHE VAL MET ASP GLY SER GLN PRO LEU          
SEQRES  10 A  203  ASP PRO ARG LYS THR ILE PHE VAL GLY GLY VAL PRO ARG          
SEQRES  11 A  203  PRO LEU ARG ALA VAL GLU LEU ALA MET ILE MET ASP ARG          
SEQRES  12 A  203  LEU TYR GLY GLY VAL CYS TYR ALA GLY ILE ASP THR ASP          
SEQRES  13 A  203  PRO GLU LEU LYS TYR PRO LYS GLY ALA GLY ARG VAL ALA          
SEQRES  14 A  203  PHE SER ASN GLN GLN SER TYR ILE ALA ALA ILE SER ALA          
SEQRES  15 A  203  ARG PHE VAL GLN LEU GLN HIS GLY GLU ILE ASP LYS ARG          
SEQRES  16 A  203  VAL GLU VAL LYS PRO TYR VAL LEU                              
HELIX    1   1 ASP A   77  PHE A   85  1                                   9    
HELIX    2   2 SER A  119  ALA A  127  1                                   9    
HELIX    3   3 ALA A  186  TYR A  197  1                                  12    
HELIX    4   4 GLN A  225  SER A  233  1                                   9    
SHEET    1   A 6 LEU A  91  ASP A  94  0                                        
SHEET    2   A 6 ALA A 111  PHE A 115 -1  O  LEU A 114   N  ILE A  92           
SHEET    3   A 6 SER A  64  VAL A  69 -1  N  VAL A  69   O  ALA A 111           
SHEET    4   A 6 VAL A 149  TRP A 154 -1  O  TRP A 154   N  SER A  64           
SHEET    5   A 6 LEU A 135  LEU A 137 -1  N  LEU A 135   O  ILE A 151           
SHEET    6   A 6 ILE A 129  GLU A 130 -1  N  ILE A 129   O  TYR A 136           
SHEET    1   B 5 ASP A 160  VAL A 162  0                                        
SHEET    2   B 5 TYR A 202  ASP A 208 -1  O  ALA A 203   N  PHE A 161           
SHEET    3   B 5 TYR A 213  ALA A 221 -1  O  ALA A 217   N  ASP A 206           
SHEET    4   B 5 THR A 174  GLY A 178 -1  N  ILE A 175   O  VAL A 220           
SHEET    5   B 5 GLU A 249  PRO A 252 -1  O  LYS A 251   N  PHE A 176           
SHEET    1   C 2 GLN A 238  HIS A 241  0                                        
SHEET    2   C 2 ILE A 244  LYS A 246 -1  O  ASP A 245   N  LEU A 239           
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                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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