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Database: PDB
Entry: 2MX6
LinkDB: 2MX6
Original site: 2MX6 
HEADER    PEPTIDE BINDING PROTEIN                 15-DEC-14   2MX6              
TITLE     COMPLEX STRUCTURE OF DVL PDZ DOMAIN WITH LIGAND                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-1;        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 248-337;                                      
COMPND   5 SYNONYM: DISHEVELLED-1, DSH HOMOLOG 1;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: (PHQ)WV PEPTIDE;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 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: DVL1, DVL;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630                                                
KEYWDS    PDZ, DVL, PEPTIDE BINDING PROTEIN                                     
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    X.ZHANG,J.J.ZHENG                                                     
REVDAT   1   30-DEC-15 2MX6    0                                                
JRNL        AUTH   X.ZHANG,J.J.ZHENG                                            
JRNL        TITL   PROTEIN-LIGAND INTERACTION DECODED BY NMR CHEMICAL SHIFT     
JRNL        TITL 2 ANALYSIS                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2MX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB104155.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.5                                
REMARK 210  IONIC STRENGTH                 : 0.1                                
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1 MM [U-100% 13C; U-100% 15N]      
REMARK 210                                   PROTEIN, 10 MM PEPTIDE, 100 MM     
REMARK 210                                   POTASSIUM PHOSPHATE, 90% H2O/10%   
REMARK 210                                   D2O                                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D 1H-13C NOESY; 2D 1H-15N HSQC;   
REMARK 210                                   3D HNCA; 3D HNCACB; 2D 1H-1H TOCSY 
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CNS                                
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS,            
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST 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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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 ASN A 271     -152.06    -91.76                                   
REMARK 500  1 ASP A 292      -82.21    -89.69                                   
REMARK 500  1 LEU A 302      -72.54   -102.69                                   
REMARK 500  1 ASN A 305       73.87     60.47                                   
REMARK 500  1 ASP A 306      -50.03     75.86                                   
REMARK 500  1 SER A 326       33.17    -90.21                                   
REMARK 500  2 ASP A 292      -72.52    -88.27                                   
REMARK 500  2 LEU A 302      -72.47   -105.47                                   
REMARK 500  2 ASN A 305       62.93     61.40                                   
REMARK 500  2 ASP A 306      -45.94     75.12                                   
REMARK 500  3 ASN A 271     -163.43    -77.57                                   
REMARK 500  3 ASP A 292      -77.12    -86.83                                   
REMARK 500  3 LEU A 302      -69.09   -101.29                                   
REMARK 500  3 ASN A 305       72.90     58.83                                   
REMARK 500  3 ASP A 306      -48.40     78.30                                   
REMARK 500  3 GLU A 310        6.11    -68.73                                   
REMARK 500  3 ASN A 311       33.72   -150.25                                   
REMARK 500  4 ASP A 272      -66.13   -145.03                                   
REMARK 500  4 ASP A 292      -72.81    -86.33                                   
REMARK 500  4 LEU A 302      -71.22   -105.80                                   
REMARK 500  4 ASN A 305       75.40     59.09                                   
REMARK 500  4 ASP A 306      -58.85     76.72                                   
REMARK 500  5 MET A 256       32.00    -95.80                                   
REMARK 500  5 ASN A 271     -158.77   -174.67                                   
REMARK 500  5 PRO A 297       94.34    -61.44                                   
REMARK 500  5 LEU A 302      -73.31    -97.90                                   
REMARK 500  5 ASN A 305       65.98     61.34                                   
REMARK 500  5 ASP A 306      -52.90     74.87                                   
REMARK 500  6 ASN A 271     -151.31    -92.74                                   
REMARK 500  6 ASP A 292      -72.61    -77.11                                   
REMARK 500  6 LEU A 302      -69.07   -106.25                                   
REMARK 500  6 ASN A 305       65.69     62.88                                   
REMARK 500  6 ASP A 306      -43.67     74.69                                   
REMARK 500  7 LEU A 302      -72.57   -105.15                                   
REMARK 500  7 ASN A 305       76.61     59.21                                   
REMARK 500  7 ASP A 306      -53.37     75.21                                   
REMARK 500  7 ASN A 311       53.35   -119.44                                   
REMARK 500  8 ASN A 271     -148.51    -99.37                                   
REMARK 500  8 ASP A 292      -80.25    -94.63                                   
REMARK 500  8 LEU A 302      -77.12   -103.54                                   
REMARK 500  8 ASN A 305       70.53     58.35                                   
REMARK 500  8 ASP A 306      -53.36     76.51                                   
REMARK 500  9 ASN A 271      -76.15    -75.66                                   
REMARK 500  9 ASP A 272      -16.72   -145.29                                   
REMARK 500  9 ASP A 292      -80.20    -91.80                                   
REMARK 500  9 LEU A 302      -64.67   -102.12                                   
REMARK 500  9 ASP A 306      -51.16     76.31                                   
REMARK 500 10 ASN A 271     -149.77   -104.92                                   
REMARK 500 10 ASP A 275       43.10   -103.61                                   
REMARK 500 10 ASP A 292      -75.98    -91.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      99 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 25394   RELATED DB: BMRB                                 
DBREF  2MX6 A  248   337  UNP    P51141   DVL1_MOUSE     248    337             
DBREF  2MX6 B    1     3  PDB    2MX6     2MX6             1      3             
SEQRES   1 A   90  ASN ILE ILE THR VAL THR LEU ASN MET GLU ARG HIS HIS          
SEQRES   2 A   90  PHE LEU GLY ILE SER ILE VAL GLY GLN SER ASN ASP ARG          
SEQRES   3 A   90  GLY ASP GLY GLY ILE TYR ILE GLY SER ILE MET LYS GLY          
SEQRES   4 A   90  GLY ALA VAL ALA ALA ASP GLY ARG ILE GLU PRO GLY ASP          
SEQRES   5 A   90  MET LEU LEU GLN VAL ASN ASP VAL ASN PHE GLU ASN MET          
SEQRES   6 A   90  SER ASN ASP ASP ALA VAL ARG VAL LEU ARG GLU ILE VAL          
SEQRES   7 A   90  SER GLN THR GLY PRO ILE SER LEU THR VAL ALA LYS              
SEQRES   1 B    3  PHQ TRP VAL                                                  
HET    PHQ  B   1      17                                                       
HETNAM     PHQ BENZYL CHLOROCARBONATE                                           
FORMUL   2  PHQ    C8 H7 CL O2                                                  
HELIX    1   1 GLY A  287  GLY A  293  1                                   7    
HELIX    2   2 SER A  313  SER A  326  1                                  14    
SHEET    1   A 4 ILE A 249  LEU A 254  0                                        
SHEET    2   A 4 ILE A 331  ALA A 336 -1  O  LEU A 333   N  VAL A 252           
SHEET    3   A 4 MET A 300  VAL A 304 -1  N  GLN A 303   O  THR A 334           
SHEET    4   A 4 VAL A 307  ASN A 308 -1  O  VAL A 307   N  VAL A 304           
SHEET    1   B 2 ILE A 264  GLN A 269  0                                        
SHEET    2   B 2 GLY A 277  ILE A 283 -1  O  GLY A 281   N  SER A 265           
LINK         C1  PHQ B   1                 N   TRP B   2     1555   1555  1.33  
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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