HEADER    HYDROLASE                               27-NOV-14   XXXX              
TITLE     CRYSTAL STRUCTURE OF THE MURINE NOROVIRUS NS6 PROTEASE (INACTIVE C139A
TITLE    2 MUTANT) WITH A C-TERMINAL EXTENSION TO INCLUDE RESIDUE P1 PRIME OF   
TITLE    3 NS7                                                                  
KEYWDS    MURINE NOROVIRUS PROTEASE, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.FERNANDES,E.N.LEEN,S.CURRY                                          
JRNL        AUTH   H.FERNANDES,E.N.LEEN,H.CROMWELL,M.P.PFEIL,S.CURRY            
JRNL        TITL   STRUCTURE DETERMINATION OF MURINE NOROVIRUS NS6 PROTEASES    
JRNL        TITL 2 WITH C-TERMINAL EXTENSIONS DESIGNED TO PROBE                 
JRNL        TITL 3 PROTEASE-SUBSTRATE INTERACTIONS.                             
JRNL        REF    PEERJ                         V.   3  E798 2015              
JRNL        REFN                   ESSN 2167-8359                               
JRNL        PMID   25755927                                                     
JRNL        DOI    10.7717/PEERJ.798                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.N.LEEN,G.BAEZA,S.CURRY                                     
REMARK   1  TITL   STRUCTURE OF A MURINE NOROVIRUS NS6 PROTEASE-PRODUCT COMPLEX 
REMARK   1  TITL 2 REVEALED BY ADVENTITIOUS CRYSTALLISATION.                    
REMARK   1  REF    PLOS ONE                      V.   7 38723 2012              
REMARK   1  REFN                   ESSN 1932-6203                               
REMARK   1  PMID   22685603                                                     
REMARK   1  DOI    10.1371/JOURNAL.PONE.0038723                                 
SEQRES   1 A  185  SER ALA PRO VAL SER ILE TRP SER ARG VAL VAL GLN PHE          
SEQRES   2 A  185  GLY THR GLY TRP GLY PHE TRP VAL SER GLY HIS VAL PHE          
SEQRES   3 A  185  ILE THR ALA LYS HIS VAL ALA PRO PRO LYS GLY THR GLU          
SEQRES   4 A  185  ILE PHE GLY ARG LYS PRO GLY ASP PHE THR VAL THR SER          
SEQRES   5 A  185  SER GLY ASP PHE LEU LYS TYR TYR PHE THR SER ALA VAL          
SEQRES   6 A  185  ARG PRO ASP ILE PRO ALA MET VAL LEU GLU ASN GLY CYS          
SEQRES   7 A  185  GLN GLU GLY VAL VAL ALA SER VAL LEU VAL LYS ARG ALA          
SEQRES   8 A  185  SER GLY GLU MET LEU ALA LEU ALA VAL ARG MET GLY SER          
SEQRES   9 A  185  GLN ALA ALA ILE LYS ILE GLY SER ALA VAL VAL HIS GLY          
SEQRES  10 A  185  GLN THR GLY MET LEU LEU THR GLY SER ASN ALA LYS ALA          
SEQRES  11 A  185  GLN ASP LEU GLY THR ILE PRO GLY ASP ALA GLY CYS PRO          
SEQRES  12 A  185  TYR VAL TYR LYS LYS GLY ASN THR TRP VAL VAL ILE GLY          
SEQRES  13 A  185  VAL HIS VAL ALA ALA THR ARG SER GLY ASN THR VAL ILE          
SEQRES  14 A  185  ALA ALA THR HIS GLY GLU PRO THR LEU GLU ALA LEU GLU          
SEQRES  15 A  185  PHE GLN GLY                                                  
SEQRES   1 B  185  SER ALA PRO VAL SER ILE TRP SER ARG VAL VAL GLN PHE          
SEQRES   2 B  185  GLY THR GLY TRP GLY PHE TRP VAL SER GLY HIS VAL PHE          
SEQRES   3 B  185  ILE THR ALA LYS HIS VAL ALA PRO PRO LYS GLY THR GLU          
SEQRES   4 B  185  ILE PHE GLY ARG LYS PRO GLY ASP PHE THR VAL THR SER          
SEQRES   5 B  185  SER GLY ASP PHE LEU LYS TYR TYR PHE THR SER ALA VAL          
SEQRES   6 B  185  ARG PRO ASP ILE PRO ALA MET VAL LEU GLU ASN GLY CYS          
SEQRES   7 B  185  GLN GLU GLY VAL VAL ALA SER VAL LEU VAL LYS ARG ALA          
SEQRES   8 B  185  SER GLY GLU MET LEU ALA LEU ALA VAL ARG MET GLY SER          
SEQRES   9 B  185  GLN ALA ALA ILE LYS ILE GLY SER ALA VAL VAL HIS GLY          
SEQRES  10 B  185  GLN THR GLY MET LEU LEU THR GLY SER ASN ALA LYS ALA          
SEQRES  11 B  185  GLN ASP LEU GLY THR ILE PRO GLY ASP ALA GLY CYS PRO          
SEQRES  12 B  185  TYR VAL TYR LYS LYS GLY ASN THR TRP VAL VAL ILE GLY          
SEQRES  13 B  185  VAL HIS VAL ALA ALA THR ARG SER GLY ASN THR VAL ILE          
SEQRES  14 B  185  ALA ALA THR HIS GLY GLU PRO THR LEU GLU ALA LEU GLU          
SEQRES  15 B  185  PHE GLN GLY                                                  
SEQRES   1 C  185  SER ALA PRO VAL SER ILE TRP SER ARG VAL VAL GLN PHE          
SEQRES   2 C  185  GLY THR GLY TRP GLY PHE TRP VAL SER GLY HIS VAL PHE          
SEQRES   3 C  185  ILE THR ALA LYS HIS VAL ALA PRO PRO LYS GLY THR GLU          
SEQRES   4 C  185  ILE PHE GLY ARG LYS PRO GLY ASP PHE THR VAL THR SER          
SEQRES   5 C  185  SER GLY ASP PHE LEU LYS TYR TYR PHE THR SER ALA VAL          
SEQRES   6 C  185  ARG PRO ASP ILE PRO ALA MET VAL LEU GLU ASN GLY CYS          
SEQRES   7 C  185  GLN GLU GLY VAL VAL ALA SER VAL LEU VAL LYS ARG ALA          
SEQRES   8 C  185  SER GLY GLU MET LEU ALA LEU ALA VAL ARG MET GLY SER          
SEQRES   9 C  185  GLN ALA ALA ILE LYS ILE GLY SER ALA VAL VAL HIS GLY          
SEQRES  10 C  185  GLN THR GLY MET LEU LEU THR GLY SER ASN ALA LYS ALA          
SEQRES  11 C  185  GLN ASP LEU GLY THR ILE PRO GLY ASP ALA GLY CYS PRO          
SEQRES  12 C  185  TYR VAL TYR LYS LYS GLY ASN THR TRP VAL VAL ILE GLY          
SEQRES  13 C  185  VAL HIS VAL ALA ALA THR ARG SER GLY ASN THR VAL ILE          
SEQRES  14 C  185  ALA ALA THR HIS GLY GLU PRO THR LEU GLU ALA LEU GLU          
SEQRES  15 C  185  PHE GLN GLY                                                  
SEQRES   1 D  185  SER ALA PRO VAL SER ILE TRP SER ARG VAL VAL GLN PHE          
SEQRES   2 D  185  GLY THR GLY TRP GLY PHE TRP VAL SER GLY HIS VAL PHE          
SEQRES   3 D  185  ILE THR ALA LYS HIS VAL ALA PRO PRO LYS GLY THR GLU          
SEQRES   4 D  185  ILE PHE GLY ARG LYS PRO GLY ASP PHE THR VAL THR SER          
SEQRES   5 D  185  SER GLY ASP PHE LEU LYS TYR TYR PHE THR SER ALA VAL          
SEQRES   6 D  185  ARG PRO ASP ILE PRO ALA MET VAL LEU GLU ASN GLY CYS          
SEQRES   7 D  185  GLN GLU GLY VAL VAL ALA SER VAL LEU VAL LYS ARG ALA          
SEQRES   8 D  185  SER GLY GLU MET LEU ALA LEU ALA VAL ARG MET GLY SER          
SEQRES   9 D  185  GLN ALA ALA ILE LYS ILE GLY SER ALA VAL VAL HIS GLY          
SEQRES  10 D  185  GLN THR GLY MET LEU LEU THR GLY SER ASN ALA LYS ALA          
SEQRES  11 D  185  GLN ASP LEU GLY THR ILE PRO GLY ASP ALA GLY CYS PRO          
SEQRES  12 D  185  TYR VAL TYR LYS LYS GLY ASN THR TRP VAL VAL ILE GLY          
SEQRES  13 D  185  VAL HIS VAL ALA ALA THR ARG SER GLY ASN THR VAL ILE          
SEQRES  14 D  185  ALA ALA THR HIS GLY GLU PRO THR LEU GLU ALA LEU GLU          
SEQRES  15 D  185  PHE GLN GLY                                                  
SEQRES   1 E    5  LEU GLU PHE GLN GLY                                          
SEQRES   1 F    7  UNK UNK UNK UNK UNK UNK UNK                                  
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   7  IMD    C3 H5 N2 1+                                                  
FORMUL   8  HOH   *88(H2 O)                                                     
HELIX    1 AA1 ILE A    5  SER A    7  5                                   3    
HELIX    2 AA2 HIS A   30  ALA A   32  5                                   3    
HELIX    3 AA3 ILE B    5  SER B    7  5                                   3    
HELIX    4 AA4 HIS B   30  ALA B   32  5                                   3    
HELIX    5 AA5 ILE C    5  SER C    7  5                                   3    
HELIX    6 AA6 HIS C   30  ALA C   32  5                                   3    
HELIX    7 AA7 ILE D    5  SER D    7  5                                   3    
HELIX    8 AA8 HIS D   30  ALA D   32  5                                   3    
SHEET    1   1 1 VAL A   9  PHE A  12  0                                        
SHEET    1   2 1 GLY A  15  TRP A  19  0                                        
SHEET    1   3 1 VAL A  24  ALA A  28  0                                        
SHEET    1   4 1 PHE A  47  SER A  52  0                                        
SHEET    1   5 1 PHE A  55  PHE A  60  0                                        
SHEET    1   6 1 VAL A  72  LEU A  73  0                                        
SHEET    1   7 1 VAL A  82  LYS A  88  0                                        
SHEET    1   8 1 GLU A  93  ALA A 105  0                                        
SHEET    1   9 1 GLY A 116  LEU A 121  0                                        
SHEET    1  10 1 PRO A 142  LYS A 147  0                                        
SHEET    1  11 1 THR A 150  ALA A 160  0                                        
SHEET    1  12 1 THR A 166  ALA A 170  0                                        
SHEET    1  13 1 VAL B   9  PHE B  12  0                                        
SHEET    1  14 1 GLY B  15  TRP B  19  0                                        
SHEET    1  15 1 VAL B  24  ALA B  28  0                                        
SHEET    1  16 1 PHE B  47  SER B  52  0                                        
SHEET    1  17 1 PHE B  55  PHE B  60  0                                        
SHEET    1  18 1 VAL B  72  LEU B  73  0                                        
SHEET    1  19 1 VAL B  82  LYS B  88  0                                        
SHEET    1  20 1 MET B  94  ILE B 109  0                                        
SHEET    1  21 1 ALA B 112  LEU B 121  0                                        
SHEET    1  22 1 PRO B 142  LYS B 147  0                                        
SHEET    1  23 1 THR B 150  ALA B 160  0                                        
SHEET    1  24 1 THR B 166  ALA B 170  0                                        
SHEET    1  25 1 VAL C   9  PHE C  12  0                                        
SHEET    1  26 1 GLY C  15  TRP C  19  0                                        
SHEET    1  27 1 VAL C  24  ALA C  28  0                                        
SHEET    1  28 1 PHE C  47  SER C  52  0                                        
SHEET    1  29 1 PHE C  55  PHE C  60  0                                        
SHEET    1  30 1 VAL C  72  LEU C  73  0                                        
SHEET    1  31 1 VAL C  82  LYS C  88  0                                        
SHEET    1  32 1 GLU C  93  LYS C 108  0                                        
SHEET    1  33 1 VAL C 113  LEU C 121  0                                        
SHEET    1  34 1 PRO C 142  LYS C 147  0                                        
SHEET    1  35 1 THR C 150  ALA C 160  0                                        
SHEET    1  36 1 THR C 166  ALA C 170  0                                        
SHEET    1  37 1 VAL D   9  PHE D  12  0                                        
SHEET    1  38 1 GLY D  15  TRP D  19  0                                        
SHEET    1  39 1 VAL D  24  ALA D  28  0                                        
SHEET    1  40 1 PHE D  47  SER D  52  0                                        
SHEET    1  41 1 PHE D  55  PHE D  60  0                                        
SHEET    1  42 1 VAL D  72  LEU D  73  0                                        
SHEET    1  43 1 VAL D  82  LYS D  88  0                                        
SHEET    1  44 1 MET D  94  ALA D 106  0                                        
SHEET    1  45 1 HIS D 115  LEU D 121  0                                        
SHEET    1  46 1 PRO D 142  LYS D 147  0                                        
SHEET    1  47 1 THR D 150  ALA D 160  0                                        
SHEET    1  48 1 THR D 166  ALA D 170  0                                        
LINK         C   UNK F   1                 N   UNK F   2     1555   1555  1.34  
LINK         C   UNK F   2                 N   UNK F   3     1555   1555  1.35  
LINK         C   UNK F   3                 N   UNK F   4     1555   1555  1.32  
LINK         C   UNK F   4                 N   UNK F   5     1555   1555  1.32  
LINK         C   UNK F   5                 N   UNK F   6     1555   1555  1.34  
LINK         C   UNK F   6                 N   UNK F   7     1555   1555  1.33  
SITE     1 AC1  5 GLY A 124  SER A 125  ARG B 100  SER C 125                    
SITE     2 AC1  5 ARG D 100                                                     
CRYST1   99.640  111.860   81.290  90.00 119.24  90.00 C 1 2 1      16          
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      0.010036  0.000000  0.005618        0.00000                         
SCALE2      0.000000  0.008940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014098        0.00000                         
MODEL        1                                                                  
ATOM      1  N   LEU E 180     -40.354  22.917  96.953  1.00 37.96           N  
ATOM      2  CA  LEU E 180     -40.678  21.976  95.766  1.00 38.48           C  
ATOM      3  C   LEU E 180     -40.390  22.602  94.397  1.00 36.12           C  
ATOM      4  O   LEU E 180     -41.183  23.412  93.901  1.00 36.98           O  
ATOM      5  CB  LEU E 180     -42.154  21.505  95.760  1.00 35.55           C  
ATOM      6  CG  LEU E 180     -42.595  20.540  96.874  1.00 36.06           C  
ATOM      7  CD1 LEU E 180     -44.006  19.938  96.726  1.00 35.02           C  
ATOM      8  CD2 LEU E 180     -41.559  19.453  96.995  1.00 35.77           C  
ATOM      9  N   GLU E 181     -39.252  22.221  93.819  1.00 36.86           N  
ATOM     10  CA  GLU E 181     -38.938  22.423  92.382  1.00 41.27           C  
ATOM     11  C   GLU E 181     -39.874  21.672  91.425  1.00 42.76           C  
ATOM     12  O   GLU E 181     -40.031  20.447  91.524  1.00 43.01           O  
ATOM     13  CB  GLU E 181     -37.486  21.974  92.104  1.00 41.88           C  
ATOM     14  CG  GLU E 181     -36.765  22.623  90.931  1.00 42.60           C  
ATOM     15  CD  GLU E 181     -35.295  22.172  90.836  1.00 50.09           C  
ATOM     16  OE1 GLU E 181     -34.829  21.378  91.713  1.00 54.66           O  
ATOM     17  OE2 GLU E 181     -34.596  22.569  89.864  1.00 48.54           O  
ATOM     18  N   PHE E 182     -40.482  22.415  90.505  1.00 40.77           N  
ATOM     19  CA  PHE E 182     -41.271  21.826  89.429  1.00 41.62           C  
ATOM     20  C   PHE E 182     -40.649  22.139  88.090  1.00 44.03           C  
ATOM     21  O   PHE E 182     -39.701  22.929  87.983  1.00 43.85           O  
ATOM     22  CB  PHE E 182     -42.695  22.337  89.417  1.00 39.85           C  
ATOM     23  CG  PHE E 182     -43.524  21.850  90.558  1.00 43.60           C  
ATOM     24  CD1 PHE E 182     -43.476  22.477  91.790  1.00 46.49           C  
ATOM     25  CD2 PHE E 182     -44.409  20.808  90.393  1.00 48.28           C  
ATOM     26  CE1 PHE E 182     -44.288  22.060  92.836  1.00 48.09           C  
ATOM     27  CE2 PHE E 182     -45.214  20.376  91.442  1.00 51.25           C  
ATOM     28  CZ  PHE E 182     -45.149  21.000  92.666  1.00 46.04           C  
ATOM     29  N   GLN E 183     -41.186  21.459  87.082  1.00 50.57           N  
ATOM     30  CA  GLN E 183     -40.774  21.595  85.694  1.00 48.17           C  
ATOM     31  C   GLN E 183     -41.579  22.741  85.109  1.00 50.61           C  
ATOM     32  O   GLN E 183     -42.827  22.741  85.240  1.00 43.83           O  
ATOM     33  CB  GLN E 183     -41.082  20.292  84.916  1.00 47.72           C  
ATOM     34  CG  GLN E 183     -40.711  20.329  83.431  1.00 46.82           C  
ATOM     35  CD  GLN E 183     -39.241  19.985  83.124  1.00 50.07           C  
ATOM     36  OE1 GLN E 183     -38.996  19.266  82.163  1.00 59.69           O  
ATOM     37  NE2 GLN E 183     -38.266  20.493  83.911  1.00 46.99           N  
ATOM     38  N   GLY E 184     -40.876  23.709  84.493  1.00 52.88           N  
ATOM     39  CA  GLY E 184     -41.527  24.765  83.700  1.00 61.56           C  
ATOM     40  C   GLY E 184     -42.453  24.189  82.627  1.00 59.20           C  
ATOM     41  O   GLY E 184     -43.496  24.772  82.286  1.00 57.46           O  
TER      42      GLY E 184                                                      
HETATM   43  O   HOH E 201     -38.582  18.817  78.099  1.00 38.03           O  
ENDMDL                                                                          
MASTER       45    0    0    8   48    0    2    6   42    1    0   62          
END                                                                             
