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Database: PDB
Entry: 2EQU
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Original site: 2EQU 
HEADER    PROTEIN BINDING                         30-MAR-07   2EQU              
TITLE     SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN 20-LIKE 1
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHD FINGER PROTEIN 20-LIKE 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TUDOR DOMAIN;                                              
COMPND   5 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: PHF20L1;                                                       
SOURCE   6 EXPRESSION_SYSTEM: CELL-FREE PROTEIN SYNTHESIS;                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: P060911-17                                
KEYWDS    TUDOR DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON        
KEYWDS   2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL         
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING                
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    K.FUTAMI,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,        
AUTHOR   2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)    
REVDAT   3   09-MAR-22 2EQU    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 2EQU    1       VERSN                                    
REVDAT   1   02-OCT-07 2EQU    0                                                
JRNL        AUTH   K.FUTAMI,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,          
JRNL        AUTH 2 M.SHIROUZU,S.YOKOYAMA                                        
JRNL        TITL   SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN 
JRNL        TITL 2 20-LIKE 1                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XWINNMR 3.5, AMBER 9                                 
REMARK   3   AUTHORS     : BRUKER (XWINNMR), DAVID,A,CASE. (AMBER)              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EQU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000026994.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 120MM                              
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.17MM 13C-15N PROTEIN; 20MM D     
REMARK 210                                   -TRIS-HCL(PH7.0); 100MM NACL;      
REMARK 210                                   1MM D-DTT; 0.02% NAN3; 90% H2O,    
REMARK 210                                   10% D2O                            
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY; 3D_15N     
REMARK 210                                   -SEPARATED_NOESY                   
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE 20060702, NMRVIEW 5.0.4,   
REMARK 210                                   KUJIRA 0.9820, CYANA 2.0.17        
REMARK 210   METHOD USED                   : TORSION ANGLE DYANAMICS,           
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS, STRUCTURES   
REMARK 210                                   WITH THE LOWEST ENERGY, TARGET     
REMARK 210                                   FUNCTION                           
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 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 SER A  79       26.90     47.78                                   
REMARK 500  1 SER A  80       10.37   -148.58                                   
REMARK 500  1 SER A  82       30.25   -155.90                                   
REMARK 500  1 PHE A  85        8.65   -152.22                                   
REMARK 500  1 TRP A  97     -162.98   -121.71                                   
REMARK 500  1 ASN A 111        5.31     53.75                                   
REMARK 500  1 GLU A 113       43.02   -140.02                                   
REMARK 500  1 LYS A 141      -40.37   -131.24                                   
REMARK 500  2 TRP A  97     -150.09   -136.91                                   
REMARK 500  2 THR A 115     -169.19   -162.36                                   
REMARK 500  3 TRP A  97      -36.13   -144.92                                   
REMARK 500  3 LYS A 112       89.22    -29.62                                   
REMARK 500  3 GLU A 113       40.33     38.39                                   
REMARK 500  3 ALA A 140      153.86    -49.28                                   
REMARK 500  3 ASP A 144       36.47   -148.95                                   
REMARK 500  3 TRP A 145       46.67    -69.23                                   
REMARK 500  3 LEU A 148       32.39    -79.90                                   
REMARK 500  4 TRP A 145       13.81   -141.59                                   
REMARK 500  5 TRP A  97      -44.13   -140.23                                   
REMARK 500  5 GLU A 113       35.43   -142.91                                   
REMARK 500  5 TRP A 145       31.77    -69.95                                   
REMARK 500  5 LEU A 148        0.75    -67.60                                   
REMARK 500  6 TRP A  97      -48.02   -138.89                                   
REMARK 500  6 THR A  98      -14.55   -140.27                                   
REMARK 500  6 LYS A 112     -175.86    -67.24                                   
REMARK 500  6 TRP A 145       36.06    -78.13                                   
REMARK 500  7 THR A  98      -29.17   -155.25                                   
REMARK 500  7 GLU A 113       24.33   -140.63                                   
REMARK 500  7 GLN A 143        1.21    -59.61                                   
REMARK 500  7 TRP A 145        7.84     44.86                                   
REMARK 500  8 TRP A  97      -39.77   -151.42                                   
REMARK 500  8 THR A  98      -32.68   -132.73                                   
REMARK 500  8 ASN A 111       11.32     53.35                                   
REMARK 500  8 GLU A 113       49.77   -142.09                                   
REMARK 500  8 TRP A 145      -12.14   -142.51                                   
REMARK 500  9 CYS A 100       34.78    -74.04                                   
REMARK 500  9 MET A 131        2.61    -69.16                                   
REMARK 500  9 LEU A 148        2.84    -65.53                                   
REMARK 500 10 SER A  80       42.60    -80.61                                   
REMARK 500 10 TRP A  97      -42.51   -142.74                                   
REMARK 500 10 ASN A 111       18.51     51.51                                   
REMARK 500 10 MET A 131       -7.33    -59.31                                   
REMARK 500 10 LEU A 148       23.24   -152.24                                   
REMARK 500 11 TRP A  97     -159.70    -93.75                                   
REMARK 500 11 ALA A 140       89.79    -46.84                                   
REMARK 500 11 LYS A 141       27.24     45.81                                   
REMARK 500 11 TRP A 145       38.92    -81.78                                   
REMARK 500 11 ILE A 146     -149.06    -85.93                                   
REMARK 500 11 ALA A 147       48.32    -72.02                                   
REMARK 500 12 THR A  98      -56.50   -142.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      92 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HSO003013074.2   RELATED DB: TARGETDB                    
DBREF  2EQU A   85   151  UNP    Q96BT0   Q96BT0_HUMAN    85    151             
SEQADV 2EQU GLY A   78  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU SER A   79  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU SER A   80  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU GLY A   81  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU SER A   82  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU SER A   83  UNP  Q96BT0              EXPRESSION TAG                 
SEQADV 2EQU GLY A   84  UNP  Q96BT0              EXPRESSION TAG                 
SEQRES   1 A   74  GLY SER SER GLY SER SER GLY PHE ASP PHE LYS ALA GLY          
SEQRES   2 A   74  GLU GLU VAL LEU ALA ARG TRP THR ASP CYS ARG TYR TYR          
SEQRES   3 A   74  PRO ALA LYS ILE GLU ALA ILE ASN LYS GLU GLY THR PHE          
SEQRES   4 A   74  THR VAL GLN PHE TYR ASP GLY VAL ILE ARG CYS LEU LYS          
SEQRES   5 A   74  ARG MET HIS ILE LYS ALA MET PRO GLU ASP ALA LYS GLY          
SEQRES   6 A   74  GLN ASP TRP ILE ALA LEU VAL LYS ALA                          
HELIX    1   1 LYS A  129  MET A  131  5                                   3    
HELIX    2   2 PRO A  137  LYS A  141  5                                   5    
SHEET    1   A 5 ILE A 125  LEU A 128  0                                        
SHEET    2   A 5 PHE A 116  PHE A 120 -1  N  PHE A 116   O  LEU A 128           
SHEET    3   A 5 TYR A 102  ILE A 110 -1  N  GLU A 108   O  THR A 117           
SHEET    4   A 5 GLU A  92  ARG A  96 -1  N  VAL A  93   O  ALA A 105           
SHEET    5   A 5 ILE A 133  LYS A 134 -1  O  LYS A 134   N  LEU A  94           
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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