HEADER    LIGASE/SIGNALING PROTEIN                03-JAN-08   XXXX              
TITLE     CRYSTAL STRUCTURE OF C-CBL-TKB DOMAIN COMPLEXED WITH ITS              
TITLE    2 BINDING MOTIF IN C-MET                                               
COMPND    13-meric peptide from Hepatocyte growth factor receptor, E3           
COMPND   2 ubiquitin-protein ligase CBL (E.C.6.3.2.-)                           
KEYWDS    CBL, TKB, LIGASE, SIGNAL TRANSDUCTION, PROTO-ONCOGENE,                
KEYWDS   2 COMPLEX, ATP-BINDING, GLYCOPROTEIN, KINASE, MEMBRANE,                
KEYWDS   3 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, RECEPTOR, TRANSFERASE,           
KEYWDS   4 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, CALCIUM, CYTOPLASM,          
KEYWDS   5 METAL-BINDING, SH2 DOMAIN, UBL CONJUGATION PATHWAY, ZINC,            
KEYWDS   6 ZINC-FINGER, LIGASE/SIGNALING PROTEIN COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.NG, R.A.JACKSON, J.P.BUSCHDORF, Q.SUN, G.R.GUY,                     
AUTHOR   2 J.SIVARAMAN                                                          
JRNL        AUTH   C.NG, R.A.JACKSON, J.P.BUSCHDORF, Q.SUN, G.R.GUY,            
JRNL        AUTH 2 J.SIVARAMAN                                                  
JRNL        TITL   STRUCTURAL BASIS FOR A NOVEL INTRAPEPTIDYL H-BOND            
JRNL        TITL 2 AND REVERSE BINDING OF C-CBL-TKB DOMAIN SUBSTRATES           
JRNL        REF    EMBO J.                       V.  27   804 2008              
JRNL        REFN   ASTM EMJODG  UK ISSN 0261-4189                               
JRNL        PMID   18273061                                                     
JRNL        DOI    10.1038/EMBOJ.2008.18                                        
SEQRES   1 A   13  SER ASN GLU SER VAL ASP PTR ARG ALA THR PHE PRO GLU          
SEQRES   1 B  329  GLY SER LEU ILE GLY LEU MET LYS ASP ALA PHE GLN PRO          
SEQRES   2 B  329  HIS HIS HIS HIS HIS HIS HIS LEU SER PRO HIS PRO PRO          
SEQRES   3 B  329  GLY THR VAL ASP LYS LYS MET VAL GLU LYS CYS TRP LYS          
SEQRES   4 B  329  LEU MET ASP LYS VAL VAL ARG LEU CYS GLN ASN PRO LYS          
SEQRES   5 B  329  LEU ALA LEU LYS ASN SER PRO PRO TYR ILE LEU ASP LEU          
SEQRES   6 B  329  LEU PRO ASP THR TYR GLN HIS LEU ARG THR ILE LEU SER          
SEQRES   7 B  329  ARG TYR GLU GLY LYS MET GLU THR LEU GLY GLU ASN GLU          
SEQRES   8 B  329  TYR PHE ARG VAL PHE MET GLU ASN LEU MET LYS LYS THR          
SEQRES   9 B  329  LYS GLN THR ILE SER LEU PHE LYS GLU GLY LYS GLU ARG          
SEQRES  10 B  329  MET TYR GLU GLU ASN SER GLN PRO ARG ARG ASN LEU THR          
SEQRES  11 B  329  LYS LEU SER LEU ILE PHE SER HIS MET LEU ALA GLU LEU          
SEQRES  12 B  329  LYS GLY ILE PHE PRO SER GLY LEU PHE GLN GLY ASP THR          
SEQRES  13 B  329  PHE ARG ILE THR LYS ALA ASP ALA ALA GLU PHE TRP ARG          
SEQRES  14 B  329  LYS ALA PHE GLY GLU LYS THR ILE VAL PRO TRP LYS SER          
SEQRES  15 B  329  PHE ARG GLN ALA LEU HIS GLU VAL HIS PRO ILE SER SER          
SEQRES  16 B  329  GLY LEU GLU ALA MET ALA LEU LYS SER THR ILE ASP LEU          
SEQRES  17 B  329  THR CYS ASN ASP TYR ILE SER VAL PHE GLU PHE ASP ILE          
SEQRES  18 B  329  PHE THR ARG LEU PHE GLN PRO TRP SER SER LEU LEU ARG          
SEQRES  19 B  329  ASN TRP ASN SER LEU ALA VAL THR HIS PRO GLY TYR MET          
SEQRES  20 B  329  ALA PHE LEU THR TYR ASP GLU VAL LYS ALA ARG LEU GLN          
SEQRES  21 B  329  LYS PHE ILE HIS LYS PRO GLY SER TYR ILE PHE ARG LEU          
SEQRES  22 B  329  SER CYS THR ARG LEU GLY GLN TRP ALA ILE GLY TYR VAL          
SEQRES  23 B  329  THR ALA ASP GLY ASN ILE LEU GLN THR ILE PRO HIS ASN          
SEQRES  24 B  329  LYS PRO LEU PHE GLN ALA LEU ILE ASP GLY PHE ARG GLU          
SEQRES  25 B  329  GLY PHE TYR LEU PHE PRO ASP GLY ARG ASN GLN ASN PRO          
SEQRES  26 B  329  ASP LEU THR GLY                                              
SEQRES   1 C   13  SER ASN GLU SER VAL ASP PTR ARG ALA THR PHE PRO GLU          
SEQRES   1 D  329  GLY SER LEU ILE GLY LEU MET LYS ASP ALA PHE GLN PRO          
SEQRES   2 D  329  HIS HIS HIS HIS HIS HIS HIS LEU SER PRO HIS PRO PRO          
SEQRES   3 D  329  GLY THR VAL ASP LYS LYS MET VAL GLU LYS CYS TRP LYS          
SEQRES   4 D  329  LEU MET ASP LYS VAL VAL ARG LEU CYS GLN ASN PRO LYS          
SEQRES   5 D  329  LEU ALA LEU LYS ASN SER PRO PRO TYR ILE LEU ASP LEU          
SEQRES   6 D  329  LEU PRO ASP THR TYR GLN HIS LEU ARG THR ILE LEU SER          
SEQRES   7 D  329  ARG TYR GLU GLY LYS MET GLU THR LEU GLY GLU ASN GLU          
SEQRES   8 D  329  TYR PHE ARG VAL PHE MET GLU ASN LEU MET LYS LYS THR          
SEQRES   9 D  329  LYS GLN THR ILE SER LEU PHE LYS GLU GLY LYS GLU ARG          
SEQRES  10 D  329  MET TYR GLU GLU ASN SER GLN PRO ARG ARG ASN LEU THR          
SEQRES  11 D  329  LYS LEU SER LEU ILE PHE SER HIS MET LEU ALA GLU LEU          
SEQRES  12 D  329  LYS GLY ILE PHE PRO SER GLY LEU PHE GLN GLY ASP THR          
SEQRES  13 D  329  PHE ARG ILE THR LYS ALA ASP ALA ALA GLU PHE TRP ARG          
SEQRES  14 D  329  LYS ALA PHE GLY GLU LYS THR ILE VAL PRO TRP LYS SER          
SEQRES  15 D  329  PHE ARG GLN ALA LEU HIS GLU VAL HIS PRO ILE SER SER          
SEQRES  16 D  329  GLY LEU GLU ALA MET ALA LEU LYS SER THR ILE ASP LEU          
SEQRES  17 D  329  THR CYS ASN ASP TYR ILE SER VAL PHE GLU PHE ASP ILE          
SEQRES  18 D  329  PHE THR ARG LEU PHE GLN PRO TRP SER SER LEU LEU ARG          
SEQRES  19 D  329  ASN TRP ASN SER LEU ALA VAL THR HIS PRO GLY TYR MET          
SEQRES  20 D  329  ALA PHE LEU THR TYR ASP GLU VAL LYS ALA ARG LEU GLN          
SEQRES  21 D  329  LYS PHE ILE HIS LYS PRO GLY SER TYR ILE PHE ARG LEU          
SEQRES  22 D  329  SER CYS THR ARG LEU GLY GLN TRP ALA ILE GLY TYR VAL          
SEQRES  23 D  329  THR ALA ASP GLY ASN ILE LEU GLN THR ILE PRO HIS ASN          
SEQRES  24 D  329  LYS PRO LEU PHE GLN ALA LEU ILE ASP GLY PHE ARG GLU          
SEQRES  25 D  329  GLY PHE TYR LEU PHE PRO ASP GLY ARG ASN GLN ASN PRO          
SEQRES  26 D  329  ASP LEU THR GLY                                              
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   5  HOH   *686(H2 O)                                                    
HELIX    1   1 ASP B   52  GLN B   71  1                                  20    
HELIX    2   2 ASN B   72  ALA B   76  5                                   5    
HELIX    3   3 TYR B   83  TYR B  102  1                                  20    
HELIX    4   4 LYS B  105  ASN B  112  1                                   8    
HELIX    5   5 ASN B  112  LYS B  137  1                                  26    
HELIX    6   6 GLU B  138  GLU B  142  5                                   5    
HELIX    7   7 SER B  145  PHE B  169  1                                  25    
HELIX    8   8 PRO B  170  LEU B  173  5                                   4    
HELIX    9   9 GLN B  175  PHE B  179  5                                   5    
HELIX   10  10 LYS B  183  GLY B  195  1                                  13    
HELIX   11  11 TRP B  202  HIS B  213  1                                  12    
HELIX   12  12 SER B  217  ASP B  229  1                                  13    
HELIX   13  13 VAL B  238  PHE B  248  1                                  11    
HELIX   14  14 PRO B  250  SER B  252  5                                   3    
HELIX   15  15 SER B  253  ALA B  262  1                                  10    
HELIX   16  16 THR B  273  GLN B  282  1                                  10    
HELIX   17  17 LYS B  283  ILE B  285  5                                   3    
HELIX   18  18 PRO B  323  GLU B  334  1                                  12    
HELIX   19  19 ASP D   52  GLN D   71  1                                  20    
HELIX   20  20 ASN D   72  ALA D   76  5                                   5    
HELIX   21  21 TYR D   83  TYR D  102  1                                  20    
HELIX   22  22 LYS D  105  ASN D  112  1                                   8    
HELIX   23  23 ASN D  112  LYS D  137  1                                  26    
HELIX   24  24 GLU D  138  GLU D  142  5                                   5    
HELIX   25  25 SER D  145  PHE D  169  1                                  25    
HELIX   26  26 PRO D  170  LEU D  173  5                                   4    
HELIX   27  27 GLN D  175  PHE D  179  5                                   5    
HELIX   28  28 LYS D  183  GLY D  195  1                                  13    
HELIX   29  29 TRP D  202  HIS D  213  1                                  12    
HELIX   30  30 SER D  217  ASP D  229  1                                  13    
HELIX   31  31 VAL D  238  PHE D  248  1                                  11    
HELIX   32  32 PRO D  250  SER D  252  5                                   3    
HELIX   33  33 SER D  253  ALA D  262  1                                  10    
HELIX   34  34 THR D  273  GLN D  282  1                                  10    
HELIX   35  35 LYS D  283  ILE D  285  5                                   3    
HELIX   36  36 PRO D  323  GLU D  334  1                                  12    
SHEET    1   A 2 ILE B 199  PRO B 201  0                                        
SHEET    2   A 2 TYR B 235  SER B 237 -1  O  ILE B 236   N  VAL B 200           
SHEET    1   B 4 ILE B 314  THR B 317  0                                        
SHEET    2   B 4 TRP B 303  VAL B 308 -1  N  ILE B 305   O  THR B 317           
SHEET    3   B 4 SER B 290  LEU B 295 -1  N  ARG B 294   O  ALA B 304           
SHEET    4   B 4 PHE B 339  PRO B 340  1  O  PHE B 339   N  TYR B 291           
SHEET    1   C 2 ILE D 199  PRO D 201  0                                        
SHEET    2   C 2 TYR D 235  SER D 237 -1  O  ILE D 236   N  VAL D 200           
SHEET    1   D 4 ILE D 314  THR D 317  0                                        
SHEET    2   D 4 TRP D 303  VAL D 308 -1  N  ILE D 305   O  THR D 317           
SHEET    3   D 4 SER D 290  LEU D 295 -1  N  ARG D 294   O  ALA D 304           
SHEET    4   D 4 PHE D 339  PRO D 340  1  O  PHE D 339   N  TYR D 291           
LINK         C   ASP A1002                 N   PTR A1003     1555   1555  1.33  
LINK         C   PTR A1003                 N   ARG A1004     1555   1555  1.33  
LINK         C   ASP C1002                 N   PTR C1003     1555   1555  1.33  
LINK         C   PTR C1003                 N   ARG C1004     1555   1555  1.33  
CISPEP   1 PRO B   81    PRO B   82          1        -0.19                     
CISPEP   2 GLN B  249    PRO B  250          1         1.31                     
CISPEP   3 PRO D   81    PRO D   82          1        -0.07                     
CISPEP   4 GLN D  249    PRO D  250          1         0.74                     
CRYST1   63.175  104.800   52.598  90.00  90.41  90.00 P 1 21 1      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      0.015829  0.000000  0.000113        0.00000                         
SCALE2      0.000000  0.009542  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019013        0.00000                         
MODEL        1                                                                  
ATOM      1  N   ASN C 998      44.277  16.381   0.426  1.00 34.46           N  
ATOM      2  CA  ASN C 998      43.545  15.111   0.134  1.00 34.40           C  
ATOM      3  C   ASN C 998      42.459  15.333  -0.916  1.00 34.11           C  
ATOM      4  O   ASN C 998      42.279  14.516  -1.829  1.00 35.17           O  
ATOM      5  CB  ASN C 998      42.890  14.585   1.420  1.00 34.35           C  
ATOM      6  CG  ASN C 998      43.867  14.448   2.568  1.00 32.24           C  
ATOM      7  OD1 ASN C 998      44.870  13.742   2.466  1.00 34.40           O  
ATOM      8  ND2 ASN C 998      43.569  15.124   3.683  1.00 34.04           N  
ATOM      9  N   GLU C 999      41.751  16.451  -0.767  1.00 34.54           N  
ATOM     10  CA  GLU C 999      40.650  16.795  -1.641  1.00 33.40           C  
ATOM     11  C   GLU C 999      40.848  16.560  -3.142  1.00 32.84           C  
ATOM     12  O   GLU C 999      39.878  16.574  -3.897  1.00 33.06           O  
ATOM     13  CB  GLU C 999      40.208  18.246  -1.391  1.00 34.36           C  
ATOM     14  CG  GLU C 999      39.566  18.438  -0.029  1.00 34.76           C  
ATOM     15  CD  GLU C 999      39.162  19.878   0.236  1.00 35.18           C  
ATOM     16  OE1 GLU C 999      40.050  20.757   0.266  1.00 36.18           O  
ATOM     17  OE2 GLU C 999      37.955  20.128   0.412  1.00 35.07           O  
ATOM     18  N   SER C1000      42.084  16.330  -3.576  1.00 31.25           N  
ATOM     19  CA  SER C1000      42.347  16.114  -4.992  1.00 29.27           C  
ATOM     20  C   SER C1000      42.834  14.715  -5.372  1.00 27.65           C  
ATOM     21  O   SER C1000      43.005  14.418  -6.557  1.00 27.60           O  
ATOM     22  CB  SER C1000      43.356  17.148  -5.495  1.00 30.33           C  
ATOM     23  OG  SER C1000      44.601  17.021  -4.835  1.00 31.33           O  
ATOM     24  N   VAL C1001      43.060  13.861  -4.381  1.00 25.55           N  
ATOM     25  CA  VAL C1001      43.531  12.512  -4.653  1.00 23.43           C  
ATOM     26  C   VAL C1001      42.857  11.420  -3.812  1.00 20.91           C  
ATOM     27  O   VAL C1001      42.795  11.516  -2.585  1.00 21.64           O  
ATOM     28  CB  VAL C1001      45.062  12.424  -4.463  1.00 23.94           C  
ATOM     29  CG1 VAL C1001      45.426  12.717  -3.013  1.00 25.25           C  
ATOM     30  CG2 VAL C1001      45.562  11.050  -4.889  1.00 24.16           C  
ATOM     31  N   ASP C1002      42.356  10.390  -4.486  1.00 18.06           N  
ATOM     32  CA  ASP C1002      41.677   9.279  -3.827  1.00 16.91           C  
ATOM     33  C   ASP C1002      42.537   8.607  -2.756  1.00 17.03           C  
ATOM     34  O   ASP C1002      43.735   8.388  -2.976  1.00 16.93           O  
ATOM     35  CB  ASP C1002      41.272   8.247  -4.876  1.00 15.70           C  
ATOM     36  CG  ASP C1002      40.243   7.264  -4.363  1.00 15.81           C  
ATOM     37  OD1 ASP C1002      39.033   7.585  -4.403  1.00 13.40           O  
ATOM     38  OD2 ASP C1002      40.643   6.172  -3.912  1.00 15.93           O  
HETATM   39  N   PTR C1003      41.947   8.265  -1.610  1.00 16.29           N  
HETATM   40  CA  PTR C1003      42.747   7.647  -0.566  1.00 16.62           C  
HETATM   41  C   PTR C1003      43.225   6.229  -0.851  1.00 18.38           C  
HETATM   42  O   PTR C1003      44.053   5.692  -0.114  1.00 18.37           O  
HETATM   43  CB  PTR C1003      42.046   7.765   0.806  1.00 14.56           C  
HETATM   44  CG  PTR C1003      40.933   6.775   1.136  1.00 12.37           C  
HETATM   45  CD1 PTR C1003      39.586   7.070   0.813  1.00 11.27           C  
HETATM   46  CD2 PTR C1003      41.233   5.550   1.801  1.00 11.15           C  
HETATM   47  CE1 PTR C1003      38.576   6.143   1.157  1.00 11.39           C  
HETATM   48  CE2 PTR C1003      40.229   4.612   2.150  1.00 12.00           C  
HETATM   49  CZ  PTR C1003      38.903   4.942   1.816  1.00 10.49           C  
HETATM   50  OH  PTR C1003      37.855   4.010   2.170  1.00 10.57           O  
HETATM   51  P   PTR C1003      37.983   2.642   3.056  1.00 12.68           P  
HETATM   52  O1P PTR C1003      38.745   1.666   2.252  1.00 12.76           O  
HETATM   53  O2P PTR C1003      36.620   2.153   3.324  1.00 11.01           O  
HETATM   54  O3P PTR C1003      38.707   2.903   4.337  1.00 11.68           O  
ATOM     55  N   ARG C1004      42.710   5.633  -1.923  1.00 20.18           N  
ATOM     56  CA  ARG C1004      43.138   4.306  -2.330  1.00 20.31           C  
ATOM     57  C   ARG C1004      44.053   4.347  -3.555  1.00 22.83           C  
ATOM     58  O   ARG C1004      44.317   3.320  -4.189  1.00 23.49           O  
ATOM     59  CB  ARG C1004      41.942   3.408  -2.638  1.00 19.34           C  
ATOM     60  CG  ARG C1004      41.204   2.899  -1.419  1.00 17.19           C  
ATOM     61  CD  ARG C1004      40.308   1.743  -1.806  1.00 16.58           C  
ATOM     62  NE  ARG C1004      39.482   1.280  -0.695  1.00 14.69           N  
ATOM     63  CZ  ARG C1004      38.643   0.253  -0.778  1.00 15.83           C  
ATOM     64  NH1 ARG C1004      38.522  -0.415  -1.916  1.00 15.56           N  
ATOM     65  NH2 ARG C1004      37.921  -0.103   0.274  1.00 15.22           N  
ATOM     66  N   ALA C1005      44.530   5.544  -3.880  1.00 23.25           N  
ATOM     67  CA  ALA C1005      45.417   5.726  -5.009  1.00 25.02           C  
ATOM     68  C   ALA C1005      46.897   5.750  -4.615  1.00 25.56           C  
ATOM     69  O   ALA C1005      47.262   6.308  -3.573  1.00 26.25           O  
ATOM     70  CB  ALA C1005      45.056   7.010  -5.750  1.00 24.96           C  
TER      71      ALA C1005                                                      
HETATM   72  O   HOH C   8      34.862   0.355   2.094  1.00  8.25           O  
HETATM   73  O   HOH C  63      41.405   0.993   1.886  1.00 16.14           O  
HETATM   74  O   HOH C  83      39.904  -0.082  -4.495  1.00 22.27           O  
HETATM   75  O   HOH C 218      44.276  10.941  -0.229  1.00 30.17           O  
HETATM   76  O   HOH C 348      44.776   3.879   2.295  1.00 32.87           O  
HETATM   77  O   HOH C 353      42.981  12.611  -8.618  1.00 28.53           O  
HETATM   78  O   HOH C 388      43.403  10.051  -7.303  1.00 23.20           O  
HETATM   79  O   HOH C 454      42.397  -0.618  -0.214  1.00 25.78           O  
HETATM   80  O   HOH C 464      41.705  11.843 -10.864  1.00 32.54           O  
HETATM   81  O   HOH C 485      42.042   4.812  -6.098  1.00 30.23           O  
HETATM   82  O   HOH C 564      41.804  -2.380  -2.156  1.00 34.74           O  
HETATM   83  O   HOH C 592      46.203   8.411  -1.491  1.00 30.19           O  
HETATM   84  O   HOH C 645      44.661   0.912  -0.913  1.00 32.32           O  
ENDMDL                                                                          
MASTER        0    0    0   36   12    0    0    6 5820    4    0   54          
END                                                                             
