HEADER    SIGNALING PROTEIN                       08-MAR-01   XXXX              
TITLE     EVH1 DOMAIN FROM MURINE HOMER 2B/VESL 2                               
COMPND    HOMER 2B                                                              
KEYWDS    EVH1 DOMAIN, HOMER, VESL, X-RAY CRYSTAL STRUCTURE, BRAIN,             
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BARZIK, U.D.CARL, W.-D.SCHUBERT, J.WEHLAND, D.W.HEINZ               
JRNL        AUTH   M.BARZIK, U.D.CARL, W.D.SCHUBERT, R.FRANK,                   
JRNL        AUTH 2 J.WEHLAND, D.W.HEINZ                                         
JRNL        TITL   THE N-TERMINAL DOMAIN OF HOMER/VESL IS A NEW CLASS           
JRNL        TITL 2 II EVH1 DOMAIN.                                              
JRNL        REF    J.MOL.BIOL.                   V. 309   155 2001              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                               
JRNL        PMID   11491285                                                     
JRNL        DOI    10.1006/JMBI.2001.4640                                       
SEQRES   1 A  111  MET GLY GLU GLN PRO ILE PHE THR THR ARG ALA HIS VAL          
SEQRES   2 A  111  PHE GLN ILE ASP PRO SER THR LYS LYS ASN TRP VAL PRO          
SEQRES   3 A  111  ALA SER LYS GLN ALA VAL THR VAL SER TYR PHE TYR ASP          
SEQRES   4 A  111  VAL THR ARG ASN SER TYR ARG ILE ILE SER VAL ASP GLY          
SEQRES   5 A  111  ALA LYS VAL ILE ILE ASN SER THR ILE THR PRO ASN MET          
SEQRES   6 A  111  THR PHE THR LYS THR SER GLN LYS PHE GLY GLN TRP ALA          
SEQRES   7 A  111  ASP SER ARG ALA ASN THR VAL PHE GLY LEU GLY PHE SER          
SEQRES   8 A  111  SER GLU LEU GLN LEU THR LYS PHE ALA GLU LYS PHE GLN          
SEQRES   9 A  111  GLU VAL ARG GLU ALA ALA ARG                                  
SEQRES   1 B  111  MET GLY GLU GLN PRO ILE PHE THR THR ARG ALA HIS VAL          
SEQRES   2 B  111  PHE GLN ILE ASP PRO SER THR LYS LYS ASN TRP VAL PRO          
SEQRES   3 B  111  ALA SER LYS GLN ALA VAL THR VAL SER TYR PHE TYR ASP          
SEQRES   4 B  111  VAL THR ARG ASN SER TYR ARG ILE ILE SER VAL ASP GLY          
SEQRES   5 B  111  ALA LYS VAL ILE ILE ASN SER THR ILE THR PRO ASN MET          
SEQRES   6 B  111  THR PHE THR LYS THR SER GLN LYS PHE GLY GLN TRP ALA          
SEQRES   7 B  111  ASP SER ARG ALA ASN THR VAL PHE GLY LEU GLY PHE SER          
SEQRES   8 B  111  SER GLU LEU GLN LEU THR LYS PHE ALA GLU LYS PHE GLN          
SEQRES   9 B  111  GLU VAL ARG GLU ALA ALA ARG                                  
SEQRES   1 C  111  MET GLY GLU GLN PRO ILE PHE THR THR ARG ALA HIS VAL          
SEQRES   2 C  111  PHE GLN ILE ASP PRO SER THR LYS LYS ASN TRP VAL PRO          
SEQRES   3 C  111  ALA SER LYS GLN ALA VAL THR VAL SER TYR PHE TYR ASP          
SEQRES   4 C  111  VAL THR ARG ASN SER TYR ARG ILE ILE SER VAL ASP GLY          
SEQRES   5 C  111  ALA LYS VAL ILE ILE ASN SER THR ILE THR PRO ASN MET          
SEQRES   6 C  111  THR PHE THR LYS THR SER GLN LYS PHE GLY GLN TRP ALA          
SEQRES   7 C  111  ASP SER ARG ALA ASN THR VAL PHE GLY LEU GLY PHE SER          
SEQRES   8 C  111  SER GLU LEU GLN LEU THR LYS PHE ALA GLU LYS PHE GLN          
SEQRES   9 C  111  GLU VAL ARG GLU ALA ALA ARG                                  
SEQRES   1 D  111  MET GLY GLU GLN PRO ILE PHE THR THR ARG ALA HIS VAL          
SEQRES   2 D  111  PHE GLN ILE ASP PRO SER THR LYS LYS ASN TRP VAL PRO          
SEQRES   3 D  111  ALA SER LYS GLN ALA VAL THR VAL SER TYR PHE TYR ASP          
SEQRES   4 D  111  VAL THR ARG ASN SER TYR ARG ILE ILE SER VAL ASP GLY          
SEQRES   5 D  111  ALA LYS VAL ILE ILE ASN SER THR ILE THR PRO ASN MET          
SEQRES   6 D  111  THR PHE THR LYS THR SER GLN LYS PHE GLY GLN TRP ALA          
SEQRES   7 D  111  ASP SER ARG ALA ASN THR VAL PHE GLY LEU GLY PHE SER          
SEQRES   8 D  111  SER GLU LEU GLN LEU THR LYS PHE ALA GLU LYS PHE GLN          
SEQRES   9 D  111  GLU VAL ARG GLU ALA ALA ARG                                  
SEQRES   1 E    3  PHE ALA PHE                                                  
HETNAM     FLC CITRATE ANION                                                    
HETNAM     PHE PHENYLALANINE                                                    
FORMUL   6  FLC    2(C6 H5 O7 3-)                                               
FORMUL   8  PHE    3(C9 H11 N O2)                                               
FORMUL  11  HOH   *106(H2 O)                                                    
HELIX    1   1 SER A   92  ARG A  111  1                                  20    
HELIX    2   2 SER B   80  ASN B   83  5                                   4    
HELIX    3   3 SER B   92  ALA B  109  1                                  18    
HELIX    4   4 SER C   92  GLU C  108  1                                  17    
HELIX    5   5 SER D   92  ARG D  111  1                                  20    
SHEET    1   A 5 LYS A  54  ILE A  61  0                                        
SHEET    2   A 5 SER A  44  ASP A  51 -1  N  ILE A  47   O  SER A  59           
SHEET    3   A 5 VAL A  32  ASP A  39 -1  N  PHE A  37   O  ARG A  46           
SHEET    4   A 5 PHE A   7  GLN A  15 -1  N  ALA A  11   O  VAL A  32           
SHEET    5   A 5 VAL A  25  PRO A  26  0                                        
SHEET    1   B 7 LYS A  54  ILE A  61  0                                        
SHEET    2   B 7 SER A  44  ASP A  51 -1  N  ILE A  47   O  SER A  59           
SHEET    3   B 7 VAL A  32  ASP A  39 -1  N  PHE A  37   O  ARG A  46           
SHEET    4   B 7 PHE A   7  GLN A  15 -1  N  ALA A  11   O  VAL A  32           
SHEET    5   B 7 THR A  84  GLY A  89  0                                        
SHEET    6   B 7 PHE A  74  ASP A  79 -1  N  GLY A  75   O  LEU A  88           
SHEET    7   B 7 PHE A  67  LYS A  69 -1  N  THR A  68   O  GLN A  76           
SHEET    1   C 5 LYS B  54  THR B  60  0                                        
SHEET    2   C 5 SER B  44  ASP B  51 -1  N  ASP B  51   O  LYS B  54           
SHEET    3   C 5 VAL B  32  ASP B  39 -1  N  SER B  35   O  ILE B  48           
SHEET    4   C 5 PHE B   7  ILE B  16 -1  N  THR B   9   O  VAL B  34           
SHEET    5   C 5 VAL B  25  PRO B  26  0                                        
SHEET    1   D 7 LYS B  54  THR B  60  0                                        
SHEET    2   D 7 SER B  44  ASP B  51 -1  N  ASP B  51   O  LYS B  54           
SHEET    3   D 7 VAL B  32  ASP B  39 -1  N  SER B  35   O  ILE B  48           
SHEET    4   D 7 PHE B   7  ILE B  16 -1  N  THR B   9   O  VAL B  34           
SHEET    5   D 7 THR B  84  GLY B  89  0                                        
SHEET    6   D 7 PHE B  74  ASP B  79 -1  N  TRP B  77   O  PHE B  86           
SHEET    7   D 7 PHE B  67  LYS B  69 -1  N  THR B  68   O  GLN B  76           
SHEET    1   E 5 LYS C  54  THR C  60  0                                        
SHEET    2   E 5 SER C  44  ASP C  51 -1  N  ILE C  47   O  SER C  59           
SHEET    3   E 5 VAL C  32  ASP C  39 -1  N  PHE C  37   O  ARG C  46           
SHEET    4   E 5 PHE C   7  ILE C  16 -1  N  ALA C  11   O  VAL C  32           
SHEET    5   E 5 VAL C  25  PRO C  26  0                                        
SHEET    1   F 7 LYS C  54  THR C  60  0                                        
SHEET    2   F 7 SER C  44  ASP C  51 -1  N  ILE C  47   O  SER C  59           
SHEET    3   F 7 VAL C  32  ASP C  39 -1  N  PHE C  37   O  ARG C  46           
SHEET    4   F 7 PHE C   7  ILE C  16 -1  N  ALA C  11   O  VAL C  32           
SHEET    5   F 7 THR C  84  PHE C  90  0                                        
SHEET    6   F 7 PHE C  74  ASP C  79 -1  N  GLY C  75   O  LEU C  88           
SHEET    7   F 7 PHE C  67  SER C  71 -1  N  THR C  68   O  GLN C  76           
SHEET    1   G 5 LYS D  54  THR D  60  0                                        
SHEET    2   G 5 SER D  44  ASP D  51 -1  N  ILE D  47   O  SER D  59           
SHEET    3   G 5 VAL D  32  ASP D  39 -1  N  ASP D  39   O  SER D  44           
SHEET    4   G 5 PHE D   7  ILE D  16 -1  N  THR D   9   O  VAL D  34           
SHEET    5   G 5 VAL D  25  PRO D  26  0                                        
SHEET    1   H 7 LYS D  54  THR D  60  0                                        
SHEET    2   H 7 SER D  44  ASP D  51 -1  N  ILE D  47   O  SER D  59           
SHEET    3   H 7 VAL D  32  ASP D  39 -1  N  ASP D  39   O  SER D  44           
SHEET    4   H 7 PHE D   7  ILE D  16 -1  N  THR D   9   O  VAL D  34           
SHEET    5   H 7 THR D  84  GLY D  89  0                                        
SHEET    6   H 7 PHE D  74  ASP D  79 -1  N  TRP D  77   O  PHE D  86           
SHEET    7   H 7 PHE D  67  LYS D  69 -1  N  THR D  68   O  GLN D  76           
SITE     1 AC1  6 ARG A  42  ARG A  46  ASN A  58  ARG A  81                    
SITE     2 AC1  6 ALA A  82  HOH A 411                                          
SITE     1 AC2  5 ASN A  83  ARG B  42  ARG B  46  THR B  60                    
SITE     2 AC2  5 ARG B  81                                                     
SITE     1 AC3  4 LYS C  73  TRP D  24  THR D  70  PHE D  74                    
SITE     1 AC4  3 THR A  33  HOH A 420  HOH A 428                               
CRYST1   64.716   50.014   73.098  90.00 101.19  90.00 P 1 21 1      8          
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      0.015452  0.000000  0.003056        0.00000                         
SCALE2      0.000000  0.019994  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013945        0.00000                         
MODEL        1                                                                  
ATOM      1  N   PHE E 201      11.128  14.649  36.776  0.00 58.64           N  
ATOM      2  CA  PHE E 201      10.815  14.065  38.078  0.00 58.14           C  
ATOM      3  C   PHE E 201       9.387  13.518  38.000  0.00 58.17           C  
ATOM      4  O   PHE E 201       8.610  13.650  38.945  0.00 60.35           O  
ATOM      5  CB  PHE E 201      10.908  15.150  39.159  0.00 56.32           C  
ATOM      6  CG  PHE E 201      11.170  14.629  40.556  0.00 55.38           C  
ATOM      7  CD1 PHE E 201      10.635  13.418  40.994  0.00 53.81           C  
ATOM      8  CD2 PHE E 201      11.883  15.404  41.466  0.00 54.02           C  
ATOM      9  CE1 PHE E 201      10.805  12.995  42.315  0.00 51.93           C  
ATOM     10  CE2 PHE E 201      12.055  14.985  42.791  0.00 54.77           C  
ATOM     11  CZ  PHE E 201      11.512  13.780  43.214  0.00 50.70           C  
ATOM     12  N   ALA E 202       9.048  12.901  36.873  0.00 53.88           N  
ATOM     13  CA  ALA E 202       7.712  12.368  36.681  0.00 56.65           C  
ATOM     14  C   ALA E 202       7.398  11.193  37.606  0.00 59.77           C  
ATOM     15  O   ALA E 202       8.222  10.802  38.428  0.00 62.05           O  
ATOM     16  CB  ALA E 202       7.539  11.951  35.237  0.00 59.04           C  
ATOM     17  N   PHE E 203       6.192  10.645  37.473  0.00 61.17           N  
ATOM     18  CA  PHE E 203       5.749   9.498  38.271  0.00 61.92           C  
ATOM     19  C   PHE E 203       5.064   8.458  37.384  0.00 63.68           C  
ATOM     20  O   PHE E 203       5.255   8.437  36.164  0.00 64.86           O  
ATOM     21  CB  PHE E 203       4.776   9.937  39.368  0.00 59.77           C  
ATOM     22  CG  PHE E 203       5.445  10.389  40.630  0.00 57.65           C  
ATOM     23  CD1 PHE E 203       6.305  11.480  40.629  0.00 58.12           C  
ATOM     24  CD2 PHE E 203       5.207   9.725  41.825  0.00 56.60           C  
ATOM     25  CE1 PHE E 203       6.917  11.901  41.804  0.00 57.14           C  
ATOM     26  CE2 PHE E 203       5.813  10.139  43.005  0.00 55.92           C  
ATOM     27  CZ  PHE E 203       6.668  11.228  42.994  0.00 57.39           C  
TER      28      PHE E 203                                                      
HETATM   29  O   HOH E  60       4.435   5.890  37.980  1.00 37.60           O  
ENDMDL                                                                          
MASTER        0    0    0    5   48    0    6    6 3513    5    0   37          
END                                                                             
