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Database: PDB
Entry: 2DO7
LinkDB: 2DO7
Original site: 2DO7 
HEADER    PROTEIN BINDING                         27-APR-06   2DO7              
TITLE     SOLUTION STRUCTURE OF THE WINGED HELIX-TURN-HELIX MOTIF OF            
TITLE    2 HUMAN CUL-4B                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-4B;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: WINGED HELIX-TURN-HELIX MOTIF;                             
COMPND   5 SYNONYM: CUL-4B;                                                     
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: CUL4B, KIAA0695;                                               
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P050822-14;                               
SOURCE   8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS                           
KEYWDS    HELIX-TURN-HELIX MOTIF, STRUCTURAL GENOMICS, NPPSFA,                  
KEYWDS   2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL                
KEYWDS   3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,           
KEYWDS   4 RSGI, PROTEIN BINDING                                                
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,                 
AUTHOR   2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE           
AUTHOR   3 (RSGI)                                                               
REVDAT   2   24-FEB-09 2DO7    1       VERSN                                    
REVDAT   1   17-APR-07 2DO7    0                                                
JRNL        AUTH   S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,                   
JRNL        AUTH 2 M.SHIROUZU,S.YOKOYAMA                                        
JRNL        TITL   SOLUTION STRUCTURE OF THE WINGED HELIX-TURN-HELIX            
JRNL        TITL 2 MOTIF OF HUMAN CUL-4B                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 2.0.17                                         
REMARK   3   AUTHORS     : GUNTERT, P.                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DO7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025645.                                      
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                : 0.8MM 13C/15N-PROTEIN, 20MM D      
REMARK 210                                   -TRIS-HCL(PH7.0), 100MM NACL,      
REMARK 210                                   1MM D-DTT, 0.02% NAN3, 10% D2O     
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, 3D_        
REMARK 210                                   13C-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                 : XWINNMR 3.5, NMRPIPE               
REMARK 210                                   20031121, NMRVIEW 5.0.4,           
REMARK 210                                   KUJIRA 0.9321, OLIVIA 1.10.5,      
REMARK 210                                   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  : TARGET FUNCTION,STRUCTURES         
REMARK 210                                   WITH THE LOWEST ENERGY,            
REMARK 210                                   STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR      
REMARK 210  SPECTROSCOPY.                                                       
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 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 805       43.43     39.25                                   
REMARK 500  1 MET A 810      116.29   -172.40                                   
REMARK 500  1 GLU A 812      125.04   -172.34                                   
REMARK 500  1 SER A 819      164.52    -42.67                                   
REMARK 500  1 ILE A 832      -71.57    -73.42                                   
REMARK 500  1 LYS A 885      -38.58    -38.75                                   
REMARK 500  1 PRO A 888        1.45    -69.74                                   
REMARK 500  1 ALA A 895      140.99    -34.12                                   
REMARK 500  2 GLN A 817      107.26   -163.58                                   
REMARK 500  2 THR A 821      131.57    -37.59                                   
REMARK 500  2 ARG A 828      -71.10    -47.53                                   
REMARK 500  3 SER A 805      116.92   -166.95                                   
REMARK 500  3 THR A 820       91.73    -65.74                                   
REMARK 500  3 GLU A 822      -34.44    -34.18                                   
REMARK 500  3 ASP A 827      -37.64    -36.14                                   
REMARK 500  3 ARG A 828      -73.89    -68.79                                   
REMARK 500  3 GLN A 829      -33.44    -39.63                                   
REMARK 500  3 LYS A 864      152.81    -38.34                                   
REMARK 500  3 PRO A 888        1.12    -69.84                                   
REMARK 500  3 ALA A 895      140.70    -34.13                                   
REMARK 500  4 ASP A 827      -33.09    -38.33                                   
REMARK 500  4 ARG A 828      -70.52    -70.48                                   
REMARK 500  4 GLN A 829      -32.79    -38.58                                   
REMARK 500  4 LYS A 864      153.35    -48.48                                   
REMARK 500  4 SER A 899      112.32   -168.08                                   
REMARK 500  4 SER A 900      105.32    -59.01                                   
REMARK 500  5 SER A 802      113.53   -170.77                                   
REMARK 500  5 GLU A 812      152.95    -38.86                                   
REMARK 500  5 ARG A 828      -70.69    -72.15                                   
REMARK 500  5 ILE A 832      -72.84    -69.90                                   
REMARK 500  5 ARG A 878       32.01    -88.33                                   
REMARK 500  5 ALA A 895      143.57    -35.45                                   
REMARK 500  5 PRO A 898       86.33    -69.72                                   
REMARK 500  6 LYS A 811       97.77    -55.36                                   
REMARK 500  6 GLU A 815      135.49    -36.78                                   
REMARK 500  6 ASP A 827      -35.70    -34.45                                   
REMARK 500  6 ARG A 828      -70.39    -65.76                                   
REMARK 500  6 ALA A 895      148.14    -35.06                                   
REMARK 500  7 GLN A 809      134.88   -172.65                                   
REMARK 500  7 GLU A 812      162.16    -41.84                                   
REMARK 500  7 THR A 820      103.32    -38.12                                   
REMARK 500  7 ARG A 823      -33.12    -39.12                                   
REMARK 500  7 ARG A 828      -72.96    -62.56                                   
REMARK 500  7 LYS A 844      -32.89    -39.76                                   
REMARK 500  7 LEU A 851      -70.11    -51.45                                   
REMARK 500  7 ALA A 895      132.59    -36.80                                   
REMARK 500  7 PRO A 898        1.90    -69.75                                   
REMARK 500  7 SER A 899      103.22    -41.29                                   
REMARK 500  8 THR A 820       88.59    -56.30                                   
REMARK 500  8 ASP A 827      -33.36    -35.32                                   
REMARK 500  8 GLN A 829      -32.80    -38.30                                   
REMARK 500  8 ILE A 836      -70.23    -70.29                                   
REMARK 500  8 LYS A 844      -75.01    -35.18                                   
REMARK 500  8 ALA A 895      129.38    -34.66                                   
REMARK 500  9 SER A 802       50.02     34.92                                   
REMARK 500  9 LEU A 851      -71.32    -55.21                                   
REMARK 500  9 ALA A 895      143.85    -35.64                                   
REMARK 500 10 THR A 813      170.39    -56.40                                   
REMARK 500 10 VAL A 824      -25.54    -39.25                                   
REMARK 500 10 ASN A 887      142.06   -173.43                                   
REMARK 500 10 PRO A 888        2.60    -69.74                                   
REMARK 500 11 MET A 810      149.90   -174.48                                   
REMARK 500 11 GLU A 816      103.11    -53.91                                   
REMARK 500 11 GLN A 829      -38.06    -39.74                                   
REMARK 500 11 ALA A 895       88.72    -67.32                                   
REMARK 500 11 PRO A 898     -166.40    -69.78                                   
REMARK 500 11 SER A 899       83.23    -69.51                                   
REMARK 500 12 GLU A 812      113.88   -162.47                                   
REMARK 500 12 SER A 819      121.53   -173.05                                   
REMARK 500 12 ASP A 827      -36.44    -34.50                                   
REMARK 500 12 ARG A 828      -70.40    -67.55                                   
REMARK 500 12 GLN A 829      -31.35    -39.51                                   
REMARK 500 12 LYS A 864      154.81    -49.84                                   
REMARK 500 12 ARG A 878       31.56    -86.14                                   
REMARK 500 12 PRO A 898       97.02    -69.81                                   
REMARK 500 13 SER A 802      109.56    -44.21                                   
REMARK 500 13 ALA A 818       98.55    -56.08                                   
REMARK 500 13 ARG A 823      -33.38    -36.77                                   
REMARK 500 13 ASP A 827      -35.42    -35.07                                   
REMARK 500 13 ARG A 828      -74.64    -72.01                                   
REMARK 500 13 GLN A 829      -38.11    -39.49                                   
REMARK 500 13 LYS A 844      -36.46    -34.78                                   
REMARK 500 13 LYS A 885      -28.05    -37.55                                   
REMARK 500 13 ALA A 895      128.45    -36.65                                   
REMARK 500 14 ASP A 827      -35.08    -36.61                                   
REMARK 500 14 ARG A 828      -72.10    -67.15                                   
REMARK 500 14 GLN A 829      -30.87    -39.58                                   
REMARK 500 14 LEU A 851      -72.30    -46.55                                   
REMARK 500 14 PRO A 898       90.51    -69.72                                   
REMARK 500 15 ASP A 827      -37.34    -34.24                                   
REMARK 500 15 ARG A 828      -72.80    -61.24                                   
REMARK 500 15 GLN A 829      -33.26    -39.57                                   
REMARK 500 15 LYS A 864      153.13    -48.02                                   
REMARK 500 15 ALA A 895      108.81    -43.94                                   
REMARK 500 15 SER A 896       30.77    -91.96                                   
REMARK 500 16 GLN A 829      -35.20    -39.26                                   
REMARK 500 16 LEU A 851      -70.45    -60.46                                   
REMARK 500 16 ALA A 895      152.73    -39.86                                   
REMARK 500 16 PRO A 898       85.69    -69.72                                   
REMARK 500 17 SER A 802      144.91   -171.30                                   
REMARK 500 17 ASP A 827      -33.16    -34.44                                   
REMARK 500 17 ARG A 828      -71.73    -66.12                                   
REMARK 500 17 GLN A 829      -34.17    -39.68                                   
REMARK 500 17 LEU A 851      -71.93    -64.78                                   
REMARK 500 17 ARG A 878       34.54    -84.55                                   
REMARK 500 17 ALA A 895      151.97    -41.97                                   
REMARK 500 18 ARG A 828      -71.13    -63.39                                   
REMARK 500 18 PRO A 898       85.78    -69.80                                   
REMARK 500 19 SER A 802      -60.05   -124.58                                   
REMARK 500 19 VAL A 814       40.06    -85.43                                   
REMARK 500 19 SER A 819     -179.92    -49.53                                   
REMARK 500 19 GLU A 822      -50.51   -128.07                                   
REMARK 500 19 ASP A 827      -35.14    -34.57                                   
REMARK 500 19 ARG A 828      -70.42    -68.51                                   
REMARK 500 19 GLN A 829      -30.77    -38.04                                   
REMARK 500 19 LYS A 864      154.56    -43.87                                   
REMARK 500 19 ARG A 878       33.77    -83.02                                   
REMARK 500 19 PRO A 898       85.63    -69.71                                   
REMARK 500 20 SER A 806      -44.81   -130.16                                   
REMARK 500 20 GLU A 812       76.58   -110.61                                   
REMARK 500 20 ARG A 828      -73.87    -57.40                                   
REMARK 500 20 GLN A 829      -31.74    -38.84                                   
REMARK 500 20 VAL A 852      -37.84    -37.91                                   
REMARK 500 20 ALA A 895     -179.36    -58.50                                   
REMARK 500 20 PRO A 898     -164.97    -69.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2DO7 A  808   895  UNP    Q13620   CUL4B_HUMAN    808    895             
SEQADV 2DO7 GLY A  801  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  802  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  803  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 GLY A  804  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  805  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  806  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 GLY A  807  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  896  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 GLY A  897  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 PRO A  898  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  899  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 SER A  900  UNP  Q13620              CLONING ARTIFACT               
SEQADV 2DO7 GLY A  901  UNP  Q13620              CLONING ARTIFACT               
SEQRES   1 A  101  GLY SER SER GLY SER SER GLY ILE GLN MET LYS GLU THR          
SEQRES   2 A  101  VAL GLU GLU GLN ALA SER THR THR GLU ARG VAL PHE GLN          
SEQRES   3 A  101  ASP ARG GLN TYR GLN ILE ASP ALA ALA ILE VAL ARG ILE          
SEQRES   4 A  101  MET LYS MET ARG LYS THR LEU SER HIS ASN LEU LEU VAL          
SEQRES   5 A  101  SER GLU VAL TYR ASN GLN LEU LYS PHE PRO VAL LYS PRO          
SEQRES   6 A  101  ALA ASP LEU LYS LYS ARG ILE GLU SER LEU ILE ASP ARG          
SEQRES   7 A  101  ASP TYR MET GLU ARG ASP LYS GLU ASN PRO ASN GLN TYR          
SEQRES   8 A  101  ASN TYR ILE ALA SER GLY PRO SER SER GLY                      
HELIX    1   1 GLU A  822  ARG A  843  1                                  22    
HELIX    2   2 HIS A  848  LEU A  859  1                                  12    
HELIX    3   3 LYS A  864  ARG A  878  1                                  15    
SHEET    1   A 3 THR A 845  SER A 847  0                                        
SHEET    2   A 3 GLN A 890  TYR A 893 -1  O  TYR A 891   N  LEU A 846           
SHEET    3   A 3 MET A 881  ARG A 883 -1  N  GLU A 882   O  ASN A 892           
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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