HEADER    TRANSPORT PROTEIN/RNA BINDING PROTEIN   14-JUL-07   XXXX              
TITLE     COMPLEX OF TRANSPORTIN 1 WITH TAP NLS, CRYSTAL FORM 2                 
COMPND    Transportin-1, Nuclear RNA export factor 1                            
KEYWDS    NUCLEAR TRANSPORT, IMPORTIN, EXPORTIN, KARYOPHERIN,                   
KEYWDS   2 NUCLEOCYTOPLASMIC, TAP, NLS, TRANSPORT PROTEIN/RNA BINDING           
KEYWDS   3 PROTEIN COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.IMASAKI, T.SHIMIZU, H.HASHIMOTO, Y.HIDAKA, S.KOSE,                  
AUTHOR   2 N.IMAMOTO, M.YAMADA, M.SATO                                          
JRNL        AUTH   T.IMASAKI, T.SHIMIZU, H.HASHIMOTO, Y.HIDAKA,                 
JRNL        AUTH 2 S.KOSE, N.IMAMOTO, M.YAMADA, M.SATO                          
JRNL        TITL   STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION AND               
JRNL        TITL 2 DISSOCIATION BY HUMAN TRANSPORTIN 1                          
JRNL        REF    MOL.CELL                      V.  28    57 2007              
JRNL        REFN   ASTM MOCEFL  US ISSN 1097-2765                               
JRNL        PMID   17936704                                                     
JRNL        DOI    10.1016/J.MOLCEL.2007.08.006                                 
SEQRES   1 A  890  MET GLU TYR GLU TRP LYS PRO ASP GLU GLN GLY LEU GLN          
SEQRES   2 A  890  GLN ILE LEU GLN LEU LEU LYS GLU SER GLN SER PRO ASP          
SEQRES   3 A  890  THR THR ILE GLN ARG THR VAL GLN GLN LYS LEU GLU GLN          
SEQRES   4 A  890  LEU ASN GLN TYR PRO ASP PHE ASN ASN TYR LEU ILE PHE          
SEQRES   5 A  890  VAL LEU THR LYS LEU LYS SER GLU ASP GLU PRO THR ARG          
SEQRES   6 A  890  SER LEU SER GLY LEU ILE LEU LYS ASN ASN VAL LYS ALA          
SEQRES   7 A  890  HIS PHE GLN ASN PHE PRO ASN GLY VAL THR ASP PHE ILE          
SEQRES   8 A  890  LYS SER GLU CYS LEU ASN ASN ILE GLY ASP SER SER PRO          
SEQRES   9 A  890  LEU ILE ARG ALA THR VAL GLY ILE LEU ILE THR THR ILE          
SEQRES  10 A  890  ALA SER LYS GLY GLU LEU GLN ASN TRP PRO ASP LEU LEU          
SEQRES  11 A  890  PRO LYS LEU CYS SER LEU LEU ASP SER GLU ASP TYR ASN          
SEQRES  12 A  890  THR CYS GLU GLY ALA PHE GLY ALA LEU GLN LYS ILE CYS          
SEQRES  13 A  890  GLU ASP SER ALA GLU ILE LEU ASP SER ASP VAL LEU ASP          
SEQRES  14 A  890  ARG PRO LEU ASN ILE MET ILE PRO LYS PHE LEU GLN PHE          
SEQRES  15 A  890  PHE LYS HIS SER SER PRO LYS ILE ARG SER HIS ALA VAL          
SEQRES  16 A  890  ALA CYS VAL ASN GLN PHE ILE ILE SER ARG THR GLN ALA          
SEQRES  17 A  890  LEU MET LEU HIS ILE ASP SER PHE ILE GLU ASN LEU PHE          
SEQRES  18 A  890  ALA LEU ALA GLY ASP GLU GLU PRO GLU VAL ARG LYS ASN          
SEQRES  19 A  890  VAL CYS ARG ALA LEU VAL MET LEU LEU GLU VAL ARG MET          
SEQRES  20 A  890  ASP ARG LEU LEU PRO HIS MET HIS ASN ILE VAL GLU TYR          
SEQRES  21 A  890  MET LEU GLN ARG THR GLN ASP GLN ASP GLU ASN VAL ALA          
SEQRES  22 A  890  LEU GLU ALA CYS GLU PHE TRP LEU THR LEU ALA GLU GLN          
SEQRES  23 A  890  PRO ILE CYS LYS ASP VAL LEU VAL ARG HIS LEU PRO LYS          
SEQRES  24 A  890  LEU ILE PRO VAL LEU VAL ASN GLY MET LYS TYR SER ASP          
SEQRES  25 A  890  ILE ASP ILE ILE LEU LEU LYS GLY ASP VAL GLU GLU ASP          
SEQRES  26 A  890  GLU THR ILE PRO ASP SER GLU GLN ASP ILE ARG PRO ARG          
SEQRES  27 A  890  PHE HIS ARG SER ARG THR VAL ALA GLN GLN HIS ASP GLU          
SEQRES  28 A  890  ASP GLY ILE GLU GLU GLU ASP ASP ASP ASP ASP GLU ILE          
SEQRES  29 A  890  ASP ASP ASP ASP THR ILE SER ASP TRP ASN LEU ARG LYS          
SEQRES  30 A  890  CYS SER ALA ALA ALA LEU ASP VAL LEU ALA ASN VAL TYR          
SEQRES  31 A  890  ARG ASP GLU LEU LEU PRO HIS ILE LEU PRO LEU LEU LYS          
SEQRES  32 A  890  GLU LEU LEU PHE HIS HIS GLU TRP VAL VAL LYS GLU SER          
SEQRES  33 A  890  GLY ILE LEU VAL LEU GLY ALA ILE ALA GLU GLY CYS MET          
SEQRES  34 A  890  GLN GLY MET ILE PRO TYR LEU PRO GLU LEU ILE PRO HIS          
SEQRES  35 A  890  LEU ILE GLN CYS LEU SER ASP LYS LYS ALA LEU VAL ARG          
SEQRES  36 A  890  SER ILE THR CYS TRP THR LEU SER ARG TYR ALA HIS TRP          
SEQRES  37 A  890  VAL VAL SER GLN PRO PRO ASP THR TYR LEU LYS PRO LEU          
SEQRES  38 A  890  MET THR GLU LEU LEU LYS ARG ILE LEU ASP SER ASN LYS          
SEQRES  39 A  890  ARG VAL GLN GLU ALA ALA CYS SER ALA PHE ALA THR LEU          
SEQRES  40 A  890  GLU GLU GLU ALA CYS THR GLU LEU VAL PRO TYR LEU ALA          
SEQRES  41 A  890  TYR ILE LEU ASP THR LEU VAL PHE ALA PHE SER LYS TYR          
SEQRES  42 A  890  GLN HIS LYS ASN LEU LEU ILE LEU TYR ASP ALA ILE GLY          
SEQRES  43 A  890  THR LEU ALA ASP SER VAL GLY HIS HIS LEU ASN LYS PRO          
SEQRES  44 A  890  GLU TYR ILE GLN MET LEU MET PRO PRO LEU ILE GLN LYS          
SEQRES  45 A  890  TRP ASN MET LEU LYS ASP GLU ASP LYS ASP LEU PHE PRO          
SEQRES  46 A  890  LEU LEU GLU CYS LEU SER SER VAL ALA THR ALA LEU GLN          
SEQRES  47 A  890  SER GLY PHE LEU PRO TYR CYS GLU PRO VAL TYR GLN ARG          
SEQRES  48 A  890  CYS VAL ASN LEU VAL GLN LYS THR LEU ALA GLN ALA MET          
SEQRES  49 A  890  LEU ASN ASN ALA GLN PRO ASP GLN TYR GLU ALA PRO ASP          
SEQRES  50 A  890  LYS ASP PHE MET ILE VAL ALA LEU ASP LEU LEU SER GLY          
SEQRES  51 A  890  LEU ALA GLU GLY LEU GLY GLY ASN ILE GLU GLN LEU VAL          
SEQRES  52 A  890  ALA ARG SER ASN ILE LEU THR LEU MET TYR GLN CYS MET          
SEQRES  53 A  890  GLN ASP LYS MET PRO GLU VAL ARG GLN SER SER PHE ALA          
SEQRES  54 A  890  LEU LEU GLY ASP LEU THR LYS ALA CYS PHE GLN HIS VAL          
SEQRES  55 A  890  LYS PRO CYS ILE ALA ASP PHE MET PRO ILE LEU GLY THR          
SEQRES  56 A  890  ASN LEU ASN PRO GLU PHE ILE SER VAL CYS ASN ASN ALA          
SEQRES  57 A  890  THR TRP ALA ILE GLY GLU ILE SER ILE GLN MET GLY ILE          
SEQRES  58 A  890  GLU MET GLN PRO TYR ILE PRO MET VAL LEU HIS GLN LEU          
SEQRES  59 A  890  VAL GLU ILE ILE ASN ARG PRO ASN THR PRO LYS THR LEU          
SEQRES  60 A  890  LEU GLU ASN THR ALA ILE THR ILE GLY ARG LEU GLY TYR          
SEQRES  61 A  890  VAL CYS PRO GLN GLU VAL ALA PRO MET LEU GLN GLN PHE          
SEQRES  62 A  890  ILE ARG PRO TRP CYS THR SER LEU ARG ASN ILE ARG ASP          
SEQRES  63 A  890  ASN GLU GLU LYS ASP SER ALA PHE ARG GLY ILE CYS THR          
SEQRES  64 A  890  MET ILE SER VAL ASN PRO SER GLY VAL ILE GLN ASP PHE          
SEQRES  65 A  890  ILE PHE PHE CYS ASP ALA VAL ALA SER TRP ILE ASN PRO          
SEQRES  66 A  890  LYS ASP ASP LEU ARG ASP MET PHE CYS LYS ILE LEU HIS          
SEQRES  67 A  890  GLY PHE LYS ASN GLN VAL GLY ASP GLU ASN TRP ARG ARG          
SEQRES  68 A  890  PHE SER ASP GLN PHE PRO LEU PRO LEU LYS GLU ARG LEU          
SEQRES  69 A  890  ALA ALA PHE TYR GLY VAL                                      
SEQRES   1 B   30  GLU GLU ASP ASP GLY ASP VAL ALA MET SER ASP ALA GLN          
SEQRES   2 B   30  ASP GLY PRO ARG VAL ARG TYR ASN PRO TYR THR THR ARG          
SEQRES   3 B   30  PRO ASN ARG ARG                                              
HELIX    1   1 ASP A    8  SER A   22  1                                  15    
HELIX    2   2 ASP A   26  TYR A   43  1                                  18    
HELIX    3   3 ASP A   45  LEU A   57  1                                  13    
HELIX    4   4 ASP A   61  ALA A   78  1                                  18    
HELIX    5   5 PRO A   84  ILE A   99  1                                  16    
HELIX    6   6 SER A  103  LYS A  120  1                                  18    
HELIX    7   7 GLU A  122  TRP A  126  5                                   5    
HELIX    8   8 ASP A  128  ASP A  138  1                                  11    
HELIX    9   9 ASP A  141  SER A  159  1                                  19    
HELIX   10  10 SER A  159  ASP A  164  1                                   6    
HELIX   11  11 SER A  165  ASP A  169  5                                   5    
HELIX   12  12 PRO A  171  PHE A  182  1                                  12    
HELIX   13  13 PHE A  183  HIS A  185  5                                   3    
HELIX   14  14 SER A  187  GLN A  200  1                                  14    
HELIX   15  15 THR A  206  LEU A  211  1                                   6    
HELIX   16  16 HIS A  212  ALA A  224  1                                  13    
HELIX   17  17 GLU A  228  ARG A  246  1                                  19    
HELIX   18  18 ARG A  246  LEU A  251  1                                   6    
HELIX   19  19 HIS A  253  GLN A  266  1                                  14    
HELIX   20  20 ASP A  269  GLU A  285  1                                  17    
HELIX   21  21 ILE A  288  VAL A  294  1                                   7    
HELIX   22  22 HIS A  296  MET A  308  1                                  13    
HELIX   23  23 SER A  311  LEU A  317  1                                   7    
HELIX   24  24 ASN A  374  ARG A  391  1                                  18    
HELIX   25  25 LEU A  394  PHE A  407  1                                  14    
HELIX   26  26 GLU A  410  ILE A  424  1                                  15    
HELIX   27  27 CYS A  428  ILE A  433  1                                   6    
HELIX   28  28 TYR A  435  LEU A  447  1                                  13    
HELIX   29  29 LYS A  451  ARG A  464  1                                  14    
HELIX   30  30 TYR A  465  GLN A  472  1                                   8    
HELIX   31  31 TYR A  477  LEU A  490  1                                  14    
HELIX   32  32 ASN A  493  CYS A  512  1                                  20    
HELIX   33  33 THR A  513  PRO A  517  5                                   5    
HELIX   34  34 TYR A  518  PHE A  530  1                                  13    
HELIX   35  35 HIS A  535  GLY A  553  1                                  19    
HELIX   36  36 HIS A  554  ASN A  557  5                                   4    
HELIX   37  37 LYS A  558  ASN A  574  1                                  17    
HELIX   38  38 ASP A  582  GLN A  598  1                                  17    
HELIX   39  39 SER A  599  PRO A  603  5                                   5    
HELIX   40  40 TYR A  604  GLN A  629  1                                  26    
HELIX   41  41 ASP A  637  GLY A  656  1                                  20    
HELIX   42  42 ILE A  659  ARG A  665  1                                   7    
HELIX   43  43 ASN A  667  MET A  676  1                                  10    
HELIX   44  44 MET A  680  ASN A  716  1                                  37    
HELIX   45  45 PHE A  721  GLY A  740  1                                  20    
HELIX   46  46 ILE A  741  GLN A  744  5                                   4    
HELIX   47  47 VAL A  750  ASN A  759  1                                  10    
HELIX   48  48 PRO A  764  CYS A  782  1                                  19    
HELIX   49  49 CYS A  782  ALA A  787  1                                   6    
HELIX   50  50 MET A  789  ARG A  802  1                                  14    
HELIX   51  51 ASN A  807  SER A  822  1                                  16    
HELIX   52  52 PRO A  825  GLN A  830  1                                   6    
HELIX   53  53 ASP A  831  SER A  841  1                                  11    
HELIX   54  54 LYS A  846  PHE A  860  1                                  15    
HELIX   55  55 VAL A  864  SER A  873  1                                  10    
HELIX   56  56 ASP A  874  PHE A  876  5                                   3    
HELIX   57  57 PRO A  877  TYR A  888  1                                  12    
CRYST1  132.442  170.986   68.340  90.00  90.00  90.00 P 21 21 2     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      0.007550  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005848  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014633        0.00000                         
MODEL        1                                                                  
ATOM      1  N   VAL B  70      33.997 -36.232 -37.999  1.00 95.41           N  
ATOM      2  CA  VAL B  70      34.205 -36.947 -39.316  1.00 95.64           C  
ATOM      3  C   VAL B  70      33.285 -36.384 -40.443  1.00 95.42           C  
ATOM      4  O   VAL B  70      33.714 -35.531 -41.236  1.00 95.18           O  
ATOM      5  CB  VAL B  70      34.179 -38.541 -39.155  1.00 95.81           C  
ATOM      6  CG1 VAL B  70      32.838 -39.054 -38.551  1.00 95.83           C  
ATOM      7  CG2 VAL B  70      34.524 -39.266 -40.473  1.00 95.92           C  
ATOM      8  N   ARG B  71      32.032 -36.848 -40.486  1.00 95.13           N  
ATOM      9  CA  ARG B  71      31.025 -36.377 -41.445  1.00 94.71           C  
ATOM     10  C   ARG B  71      30.206 -35.207 -40.890  1.00 94.65           C  
ATOM     11  O   ARG B  71      30.492 -34.691 -39.813  1.00 94.70           O  
ATOM     12  CB  ARG B  71      30.090 -37.526 -41.829  1.00 94.61           C  
ATOM     13  CG  ARG B  71      30.714 -38.543 -42.755  1.00 93.67           C  
ATOM     14  CD  ARG B  71      29.995 -39.869 -42.683  1.00 92.09           C  
ATOM     15  NE  ARG B  71      30.804 -40.925 -43.283  1.00 91.79           N  
ATOM     16  CZ  ARG B  71      30.407 -42.184 -43.453  1.00 91.87           C  
ATOM     17  NH1 ARG B  71      29.191 -42.575 -43.077  1.00 92.03           N  
ATOM     18  NH2 ARG B  71      31.233 -43.058 -44.009  1.00 91.95           N  
ATOM     19  N   TYR B  72      29.184 -34.793 -41.630  1.00 94.61           N  
ATOM     20  CA  TYR B  72      28.339 -33.681 -41.210  1.00 94.56           C  
ATOM     21  C   TYR B  72      27.254 -34.119 -40.213  1.00 94.79           C  
ATOM     22  O   TYR B  72      26.659 -35.193 -40.344  1.00 94.74           O  
ATOM     23  CB  TYR B  72      27.719 -32.979 -42.430  1.00 94.31           C  
ATOM     24  CG  TYR B  72      26.724 -31.899 -42.071  1.00 93.84           C  
ATOM     25  CD1 TYR B  72      27.144 -30.598 -41.802  1.00 93.68           C  
ATOM     26  CD2 TYR B  72      25.363 -32.181 -41.990  1.00 93.26           C  
ATOM     27  CE1 TYR B  72      26.233 -29.606 -41.461  1.00 93.46           C  
ATOM     28  CE2 TYR B  72      24.449 -31.200 -41.649  1.00 93.21           C  
ATOM     29  CZ  TYR B  72      24.890 -29.916 -41.387  1.00 93.15           C  
ATOM     30  OH  TYR B  72      23.980 -28.945 -41.053  1.00 93.59           O  
ATOM     31  N   ASN B  73      27.029 -33.277 -39.211  1.00 95.03           N  
ATOM     32  CA  ASN B  73      25.933 -33.427 -38.269  1.00 95.45           C  
ATOM     33  C   ASN B  73      25.553 -32.033 -37.798  1.00 95.59           C  
ATOM     34  O   ASN B  73      26.434 -31.256 -37.442  1.00 95.68           O  
ATOM     35  CB  ASN B  73      26.341 -34.301 -37.078  1.00 95.56           C  
ATOM     36  CG  ASN B  73      26.223 -35.791 -37.373  1.00 96.24           C  
ATOM     37  OD1 ASN B  73      25.141 -36.296 -37.706  1.00 97.10           O  
ATOM     38  ND2 ASN B  73      27.340 -36.507 -37.243  1.00 96.65           N  
ATOM     39  N   PRO B  74      24.245 -31.704 -37.803  1.00 95.76           N  
ATOM     40  CA  PRO B  74      23.799 -30.349 -37.460  1.00 96.07           C  
ATOM     41  C   PRO B  74      23.867 -30.040 -35.954  1.00 96.68           C  
ATOM     42  O   PRO B  74      23.652 -28.896 -35.549  1.00 96.40           O  
ATOM     43  CB  PRO B  74      22.358 -30.325 -37.965  1.00 95.90           C  
ATOM     44  CG  PRO B  74      21.920 -31.733 -37.897  1.00 95.44           C  
ATOM     45  CD  PRO B  74      23.115 -32.591 -38.127  1.00 95.50           C  
ATOM     46  N   TYR B  75      24.167 -31.067 -35.157  1.00 97.70           N  
ATOM     47  CA  TYR B  75      24.362 -30.979 -33.701  1.00 98.69           C  
ATOM     48  C   TYR B  75      25.204 -32.185 -33.246  1.00100.11           C  
ATOM     49  O   TYR B  75      25.412 -33.122 -34.020  1.00100.33           O  
ATOM     50  CB  TYR B  75      23.010 -30.962 -32.968  1.00 98.08           C  
ATOM     51  CG  TYR B  75      22.148 -32.186 -33.230  1.00 96.32           C  
ATOM     52  CD1 TYR B  75      22.198 -33.292 -32.387  1.00 94.89           C  
ATOM     53  CD2 TYR B  75      21.291 -32.240 -34.328  1.00 94.22           C  
ATOM     54  CE1 TYR B  75      21.420 -34.413 -32.633  1.00 93.83           C  
ATOM     55  CE2 TYR B  75      20.510 -33.354 -34.577  1.00 92.64           C  
ATOM     56  CZ  TYR B  75      20.580 -34.435 -33.732  1.00 92.50           C  
ATOM     57  OH  TYR B  75      19.805 -35.541 -33.979  1.00 91.77           O  
ATOM     58  N   THR B  76      25.704 -32.151 -32.010  1.00101.92           N  
ATOM     59  CA  THR B  76      26.328 -33.333 -31.387  1.00103.78           C  
ATOM     60  C   THR B  76      25.754 -33.526 -29.985  1.00105.07           C  
ATOM     61  O   THR B  76      25.692 -32.574 -29.198  1.00105.28           O  
ATOM     62  CB  THR B  76      27.892 -33.261 -31.297  1.00103.73           C  
ATOM     63  OG1 THR B  76      28.285 -32.248 -30.359  1.00103.93           O  
ATOM     64  CG2 THR B  76      28.544 -32.990 -32.668  1.00103.87           C  
ATOM     65  N   THR B  77      25.342 -34.759 -29.684  1.00106.66           N  
ATOM     66  CA  THR B  77      24.714 -35.113 -28.399  1.00108.11           C  
ATOM     67  C   THR B  77      25.620 -34.881 -27.175  1.00109.09           C  
ATOM     68  O   THR B  77      25.135 -34.719 -26.045  1.00109.28           O  
ATOM     69  CB  THR B  77      24.167 -36.568 -28.453  1.00108.13           C  
ATOM     70  OG1 THR B  77      22.882 -36.558 -29.090  1.00108.37           O  
ATOM     71  CG2 THR B  77      24.037 -37.191 -27.062  1.00108.17           C  
ATOM     72  N   ARG B  78      26.929 -34.834 -27.417  1.00110.21           N  
ATOM     73  CA  ARG B  78      27.917 -34.586 -26.365  1.00111.18           C  
ATOM     74  C   ARG B  78      28.757 -33.315 -26.621  1.00111.48           C  
ATOM     75  O   ARG B  78      29.773 -33.368 -27.326  1.00111.51           O  
ATOM     76  CB  ARG B  78      28.793 -35.834 -26.153  1.00111.32           C  
ATOM     77  CG  ARG B  78      28.905 -36.750 -27.384  1.00112.55           C  
ATOM     78  CD  ARG B  78      30.228 -36.581 -28.121  1.00114.69           C  
ATOM     79  NE  ARG B  78      31.323 -37.204 -27.370  1.00116.56           N  
ATOM     80  CZ  ARG B  78      32.254 -36.520 -26.666  1.00117.69           C  
ATOM     81  NH1 ARG B  78      32.253 -35.167 -26.616  1.00118.12           N  
ATOM     82  NH2 ARG B  78      33.201 -37.192 -26.016  1.00118.03           N  
ATOM     83  N   PRO B  79      28.321 -32.165 -26.050  1.00111.78           N  
ATOM     84  CA  PRO B  79      29.029 -30.886 -26.201  1.00111.95           C  
ATOM     85  C   PRO B  79      30.263 -30.795 -25.302  1.00112.11           C  
ATOM     86  CB  PRO B  79      27.988 -29.859 -25.756  1.00111.97           C  
ATOM     87  CG  PRO B  79      27.168 -30.588 -24.744  1.00111.94           C  
ATOM     88  CD  PRO B  79      27.098 -32.023 -25.221  1.00111.81           C  
TER      89      PRO B  79                                                      
ENDMDL                                                                          
MASTER        0    0    0   57    0    0    0    6 6778    2    0   72          
END                                                                             
