HEADER    TRANSCRIPTION                           30-MAY-08   XXXX              
TITLE     CRYSTAL STRUCTURE OF NAD-BOUND NMRA-AREA ZINC FINGER COMPLEX          
COMPND    NITROGEN METABOLITE REPRESSION REGULATOR NMRA, NITROGEN               
COMPND   2 REGULATORY PROTEIN AREA                                              
KEYWDS    TRANSCRIPTION REGULATION, PROTEIN-PROTEIN INTERACTIONS,               
KEYWDS   2 METAL-BINDING, NITRATE ASSIMILATION, ZINC-FINGER, DNA-               
KEYWDS   3 BINDING, ZINC FINGERS, TRANSCRIPTION, ZINC, AREA, NMRA,              
KEYWDS   4 NUCLEUS, ACTIVATOR, GATA-TYPE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KOTAKA, C.JOHNSON, H.K.LAMB, A.R.HAWKINS, J.REN,                    
AUTHOR   2 D.K.STAMMERS                                                         
JRNL        AUTH   M.KOTAKA, C.JOHNSON, H.K.LAMB, A.R.HAWKINS, J.REN,           
JRNL        AUTH 2 D.K.STAMMERS                                                 
JRNL        TITL   STRUCTURAL ANALYSIS OF THE RECOGNITION OF THE                
JRNL        TITL 2 NEGATIVE REGULATOR NMRA AND DNA BY THE ZINC FINGER           
JRNL        TITL 3 FROM THE GATA-TYPE TRANSCRIPTION FACTOR AREA.                
JRNL        REF    J.MOL.BIOL.                   V. 381   373 2008              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                               
JRNL        PMID   18602114                                                     
JRNL        DOI    10.1016/J.JMB.2008.05.077                                    
SEQRES   1 A  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 A  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 A  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 A  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 A  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 A  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 A  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 A  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 A  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 A  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 A  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 A  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 A  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 A  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 A  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 A  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 A  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 A  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 A  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 A  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 A  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 A  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 A  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 A  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 A  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 A  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 A  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 A  352  LEU                                                          
SEQRES   1 B  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 B  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 B  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 B  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 B  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 B  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 B  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 B  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 B  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 B  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 B  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 B  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 B  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 B  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 B  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 B  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 B  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 B  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 B  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 B  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 B  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 B  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 B  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 B  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 B  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 B  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 B  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 B  352  LEU                                                          
SEQRES   1 C  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 C  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 C  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 C  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 C  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 C  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 C  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 C  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 C  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 C  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 C  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 C  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 C  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 C  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 C  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 C  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 C  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 C  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 C  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 C  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 C  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 C  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 C  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 C  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 C  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 C  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 C  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 C  352  LEU                                                          
SEQRES   1 D  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 D  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 D  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 D  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 D  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 D  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 D  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 D  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 D  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 D  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 D  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 D  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 D  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 D  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 D  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 D  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 D  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 D  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 D  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 D  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 D  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 D  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 D  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 D  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 D  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 D  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 D  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 E  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 E  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 E  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 E  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 E  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 E  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 E  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 E  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 E  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 E  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 E  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 E  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 E  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 E  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 E  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 E  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 E  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 E  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 E  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 E  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 E  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 E  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 E  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 E  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 E  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 E  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 E  352  LEU                                                          
SEQRES   1 F  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 F  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 F  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 F  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 F  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 F  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 F  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 F  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 F  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 F  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 F  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 F  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 F  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 F  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 F  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 F  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 F  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 F  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 F  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 F  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 F  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 F  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 F  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 F  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 F  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 F  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 F  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 F  352  LEU                                                          
SEQRES   1 G  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 G  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 G  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 G  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 G  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 G  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 G  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 G  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 G  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 G  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 G  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 G  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 G  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 G  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 G  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 G  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 G  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 G  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 G  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 G  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 G  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 G  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 G  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 G  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 G  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 G  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 G  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 G  352  LEU                                                          
SEQRES   1 H  352  MET ALA GLN GLN LYS LYS THR ILE ALA VAL VAL ASN ALA          
SEQRES   2 H  352  THR GLY ARG GLN ALA ALA SER LEU ILE ARG VAL ALA ALA          
SEQRES   3 H  352  ALA VAL GLY HIS HIS VAL ARG ALA GLN VAL HIS SER LEU          
SEQRES   4 H  352  LYS GLY LEU ILE ALA GLU GLU LEU GLN ALA ILE PRO ASN          
SEQRES   5 H  352  VAL THR LEU PHE GLN GLY PRO LEU LEU ASN ASN VAL PRO          
SEQRES   6 H  352  LEU MET ASP THR LEU PHE GLU GLY ALA HIS LEU ALA PHE          
SEQRES   7 H  352  ILE ASN THR THR SER GLN ALA GLY ASP GLU ILE ALA ILE          
SEQRES   8 H  352  GLY LYS ASP LEU ALA ASP ALA ALA LYS ARG ALA GLY THR          
SEQRES   9 H  352  ILE GLN HIS TYR ILE TYR SER SER MET PRO ASP HIS SER          
SEQRES  10 H  352  LEU TYR GLY PRO TRP PRO ALA VAL PRO MET TRP ALA PRO          
SEQRES  11 H  352  LYS PHE THR VAL GLU ASN TYR VAL ARG GLN LEU GLY LEU          
SEQRES  12 H  352  PRO SER THR PHE VAL TYR ALA GLY ILE TYR ASN ASN ASN          
SEQRES  13 H  352  PHE THR SER LEU PRO TYR PRO LEU PHE GLN MET GLU LEU          
SEQRES  14 H  352  MET PRO ASP GLY THR PHE GLU TRP HIS ALA PRO PHE ASP          
SEQRES  15 H  352  PRO ASP ILE PRO LEU PRO TRP LEU ASP ALA GLU HIS ASP          
SEQRES  16 H  352  VAL GLY PRO ALA LEU LEU GLN ILE PHE LYS ASP GLY PRO          
SEQRES  17 H  352  GLN LYS TRP ASN GLY HIS ARG ILE ALA LEU THR PHE GLU          
SEQRES  18 H  352  THR LEU SER PRO VAL GLN VAL CYS ALA ALA PHE SER ARG          
SEQRES  19 H  352  ALA LEU ASN ARG ARG VAL THR TYR VAL GLN VAL PRO LYS          
SEQRES  20 H  352  VAL GLU ILE LYS VAL ASN ILE PRO VAL GLY TYR ARG GLU          
SEQRES  21 H  352  GLN LEU GLU ALA ILE GLU VAL VAL PHE GLY GLU HIS LYS          
SEQRES  22 H  352  ALA PRO TYR PHE PRO LEU PRO GLU PHE SER ARG PRO ALA          
SEQRES  23 H  352  ALA GLY SER PRO LYS GLY LEU GLY PRO ALA ASN GLY LYS          
SEQRES  24 H  352  GLY ALA GLY ALA GLY MET MET GLN GLY PRO GLY GLY VAL          
SEQRES  25 H  352  ILE SER GLN ARG VAL THR ASP GLU ALA ARG LYS LEU TRP          
SEQRES  26 H  352  SER GLY TRP ARG ASP MET GLU GLU TYR ALA ARG GLU VAL          
SEQRES  27 H  352  PHE PRO ILE GLU GLU GLU ALA ASN GLY LEU ASP TRP MET          
SEQRES  28 H  352  LEU                                                          
SEQRES   1 I   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 I   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 I   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 I   43  PRO LEU SER LEU                                              
SEQRES   1 J   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 J   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 J   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 J   43  PRO LEU SER LEU                                              
SEQRES   1 K   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 K   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 K   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 K   43  PRO LEU SER LEU                                              
SEQRES   1 L   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 L   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 L   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 L   43  PRO LEU SER LEU                                              
SEQRES   1 M   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 M   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 M   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 M   43  PRO LEU SER LEU                                              
SEQRES   1 N   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 N   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 N   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 N   43  PRO LEU SER LEU                                              
SEQRES   1 O   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 O   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 O   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 O   43  PRO LEU SER LEU                                              
SEQRES   1 P   43  PRO THR THR CYS THR ASN CYS PHE THR GLN THR THR PRO          
SEQRES   2 P   43  LEU TRP ARG ARG ASN PRO GLU GLY GLN PRO LEU CYS ASN          
SEQRES   3 P   43  ALA CYS GLY LEU PHE LEU LYS LEU HIS GLY VAL VAL ARG          
SEQRES   4 P   43  PRO LEU SER LEU                                              
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
FORMUL  17  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  18   CL    7(CL 1-)                                                     
FORMUL  20  GOL    3(C3 H8 O3)                                                  
FORMUL  34   ZN    8(ZN 2+)                                                     
FORMUL  43  HOH   *1957(H2 O)                                                   
HELIX    1   1 GLY A   15  GLY A   29  1                                  15    
HELIX    2   2 GLY A   41  ILE A   50  1                                  10    
HELIX    3   3 ASN A   63  GLU A   72  1                                  10    
HELIX    4   4 THR A   82  GLY A   86  5                                   5    
HELIX    5   5 ASP A   87  GLY A  103  1                                  17    
HELIX    6   6 ASP A  115  TYR A  119  5                                   5    
HELIX    7   7 TRP A  128  LEU A  141  1                                  14    
HELIX    8   8 ASN A  155  PHE A  157  5                                   3    
HELIX    9   9 ASP A  191  ASN A  212  1                                  22    
HELIX   10  10 SER A  224  ASN A  237  1                                  14    
HELIX   11  11 PRO A  255  GLY A  270  1                                  16    
HELIX   12  12 THR A  318  TRP A  325  1                                   8    
HELIX   13  13 ASP A  330  VAL A  338  1                                   9    
HELIX   14  14 VAL A  338  LEU A  348  1                                  11    
HELIX   15  15 GLY B   15  GLY B   29  1                                  15    
HELIX   16  16 GLY B   41  ILE B   50  1                                  10    
HELIX   17  17 ASN B   63  GLU B   72  1                                  10    
HELIX   18  18 THR B   82  GLY B   86  5                                   5    
HELIX   19  19 ASP B   87  GLY B  103  1                                  17    
HELIX   20  20 ASP B  115  TYR B  119  5                                   5    
HELIX   21  21 TRP B  128  GLY B  142  1                                  15    
HELIX   22  22 ASN B  155  PHE B  157  5                                   3    
HELIX   23  23 ASP B  191  ASN B  212  1                                  22    
HELIX   24  24 SER B  224  ASN B  237  1                                  14    
HELIX   25  25 PRO B  255  GLU B  271  1                                  17    
HELIX   26  26 LEU B  279  SER B  283  5                                   5    
HELIX   27  27 THR B  318  TRP B  325  1                                   8    
HELIX   28  28 ASP B  330  VAL B  338  1                                   9    
HELIX   29  29 VAL B  338  ASN B  346  1                                   9    
HELIX   30  30 GLY C   15  GLY C   29  1                                  15    
HELIX   31  31 GLY C   41  ALA C   49  1                                   9    
HELIX   32  32 ASN C   63  GLU C   72  1                                  10    
HELIX   33  33 THR C   82  GLY C   86  5                                   5    
HELIX   34  34 ASP C   87  GLY C  103  1                                  17    
HELIX   35  35 ASP C  115  TYR C  119  5                                   5    
HELIX   36  36 TRP C  128  LEU C  141  1                                  14    
HELIX   37  37 ASN C  155  PHE C  157  5                                   3    
HELIX   38  38 ASP C  191  ASN C  212  1                                  22    
HELIX   39  39 SER C  224  ASN C  237  1                                  14    
HELIX   40  40 PRO C  255  GLY C  270  1                                  16    
HELIX   41  41 LEU C  279  SER C  283  5                                   5    
HELIX   42  42 THR C  318  TRP C  325  1                                   8    
HELIX   43  43 ASP C  330  VAL C  338  1                                   9    
HELIX   44  44 VAL C  338  ASN C  346  1                                   9    
HELIX   45  45 GLY D   15  GLY D   29  1                                  15    
HELIX   46  46 GLY D   41  ILE D   50  1                                  10    
HELIX   47  47 ASN D   63  PHE D   71  1                                   9    
HELIX   48  48 THR D   82  GLY D   86  5                                   5    
HELIX   49  49 ASP D   87  GLY D  103  1                                  17    
HELIX   50  50 ASP D  115  TYR D  119  5                                   5    
HELIX   51  51 TRP D  128  GLY D  142  1                                  15    
HELIX   52  52 ASN D  155  PHE D  157  5                                   3    
HELIX   53  53 ASP D  191  ASN D  212  1                                  22    
HELIX   54  54 SER D  224  ASN D  237  1                                  14    
HELIX   55  55 PRO D  255  GLU D  271  1                                  17    
HELIX   56  56 LEU D  279  SER D  283  5                                   5    
HELIX   57  57 THR D  318  TRP D  325  1                                   8    
HELIX   58  58 ASP D  330  VAL D  338  1                                   9    
HELIX   59  59 VAL D  338  ALA D  345  1                                   8    
HELIX   60  60 GLY E   15  GLY E   29  1                                  15    
HELIX   61  61 GLY E   41  ALA E   49  1                                   9    
HELIX   62  62 ASN E   63  GLU E   72  1                                  10    
HELIX   63  63 THR E   82  GLY E   86  5                                   5    
HELIX   64  64 ASP E   87  GLY E  103  1                                  17    
HELIX   65  65 ASP E  115  TYR E  119  5                                   5    
HELIX   66  66 TRP E  128  LEU E  141  1                                  14    
HELIX   67  67 ASN E  155  PHE E  157  5                                   3    
HELIX   68  68 ASP E  191  ASN E  212  1                                  22    
HELIX   69  69 SER E  224  ASN E  237  1                                  14    
HELIX   70  70 PRO E  255  PHE E  269  1                                  15    
HELIX   71  71 LEU E  279  SER E  283  5                                   5    
HELIX   72  72 THR E  318  TRP E  325  1                                   8    
HELIX   73  73 ASP E  330  VAL E  338  1                                   9    
HELIX   74  74 VAL E  338  ASN E  346  1                                   9    
HELIX   75  75 GLY F   15  GLY F   29  1                                  15    
HELIX   76  76 GLY F   41  ILE F   50  1                                  10    
HELIX   77  77 ASN F   63  GLU F   72  1                                  10    
HELIX   78  78 THR F   82  GLY F   86  5                                   5    
HELIX   79  79 ASP F   87  GLY F  103  1                                  17    
HELIX   80  80 ASP F  115  TYR F  119  5                                   5    
HELIX   81  81 TRP F  128  LEU F  141  1                                  14    
HELIX   82  82 ASN F  155  PHE F  157  5                                   3    
HELIX   83  83 ASP F  191  ASN F  212  1                                  22    
HELIX   84  84 SER F  224  ASN F  237  1                                  14    
HELIX   85  85 PRO F  255  PHE F  269  1                                  15    
HELIX   86  86 THR F  318  TRP F  325  1                                   8    
HELIX   87  87 ASP F  330  VAL F  338  1                                   9    
HELIX   88  88 VAL F  338  ASN F  346  1                                   9    
HELIX   89  89 GLY G   15  GLY G   29  1                                  15    
HELIX   90  90 GLY G   41  ILE G   50  1                                  10    
HELIX   91  91 ASN G   63  GLU G   72  1                                  10    
HELIX   92  92 ASP G   87  GLY G  103  1                                  17    
HELIX   93  93 ASP G  115  TYR G  119  5                                   5    
HELIX   94  94 TRP G  128  LEU G  141  1                                  14    
HELIX   95  95 ASN G  155  PHE G  157  5                                   3    
HELIX   96  96 ASP G  191  ASN G  212  1                                  22    
HELIX   97  97 SER G  224  ASN G  237  1                                  14    
HELIX   98  98 PRO G  255  GLY G  270  1                                  16    
HELIX   99  99 LEU G  279  SER G  283  5                                   5    
HELIX  100 100 THR G  318  TRP G  325  1                                   8    
HELIX  101 101 ASP G  330  VAL G  338  1                                   9    
HELIX  102 102 VAL G  338  ASN G  346  1                                   9    
HELIX  103 103 GLY H   15  GLY H   29  1                                  15    
HELIX  104 104 GLY H   41  ILE H   50  1                                  10    
HELIX  105 105 ASN H   63  GLU H   72  1                                  10    
HELIX  106 106 ASP H   87  GLY H  103  1                                  17    
HELIX  107 107 ASP H  115  TYR H  119  5                                   5    
HELIX  108 108 TRP H  128  LEU H  141  1                                  14    
HELIX  109 109 ASN H  155  PHE H  157  5                                   3    
HELIX  110 110 ASP H  191  ASN H  212  1                                  22    
HELIX  111 111 SER H  224  ASN H  237  1                                  14    
HELIX  112 112 PRO H  255  GLY H  270  1                                  16    
HELIX  113 113 LEU H  279  SER H  283  5                                   5    
HELIX  114 114 THR H  318  TRP H  325  1                                   8    
HELIX  115 115 ASP H  330  VAL H  338  1                                   9    
HELIX  116 116 VAL H  338  ASN H  346  1                                   9    
HELIX  117 117 CYS I  694  GLY I  705  1                                  12    
HELIX  118 118 ASN J  695  GLY J  705  1                                  11    
HELIX  119 119 ASN K  695  GLY K  705  1                                  11    
HELIX  120 120 CYS L  694  GLY L  705  1                                  12    
HELIX  121 121 CYS M  693  GLY M  704  1                                  12    
HELIX  122 122 ASN N  695  GLY N  705  1                                  11    
HELIX  123 123 ASN O  695  GLY O  705  1                                  11    
HELIX  124 124 CYS P  694  GLY P  705  1                                  12    
SHEET    1  AA 7 VAL A  53  GLN A  57  0                                        
SHEET    2  AA 7 VAL A  32  VAL A  36  1  O  VAL A  32   N  THR A  54           
SHEET    3  AA 7 ILE A   8  VAL A  10  1  O  ILE A   8   N  ARG A  33           
SHEET    4  AA 7 LEU A  76  ILE A  79  1  O  LEU A  76   N  ALA A   9           
SHEET    5  AA 7 HIS A 107  SER A 112  1  O  HIS A 107   N  ALA A  77           
SHEET    6  AA 7 SER A 145  ALA A 150  1  O  THR A 146   N  TYR A 110           
SHEET    7  AA 7 ARG A 215  LEU A 218  1  O  ILE A 216   N  TYR A 149           
SHEET    1  AB 3 ILE A 152  TYR A 153  0                                        
SHEET    2  AB 3 LEU A 187  LEU A 190  1  O  PRO A 188   N  ILE A 152           
SHEET    3  AB 3 GLU A 221  LEU A 223 -1  O  GLU A 221   N  TRP A 189           
SHEET    1  AC 3 MET A 167  LEU A 169  0                                        
SHEET    2  AC 3 PHE A 175  ALA A 179 -1  O  GLU A 176   N  GLU A 168           
SHEET    3  AC 3 VAL A 240  GLN A 244  1  O  THR A 241   N  TRP A 177           
SHEET    1  BA 7 VAL B  53  GLN B  57  0                                        
SHEET    2  BA 7 HIS B  31  VAL B  36  1  O  VAL B  32   N  THR B  54           
SHEET    3  BA 7 THR B   7  VAL B  10  1  O  ILE B   8   N  ARG B  33           
SHEET    4  BA 7 LEU B  76  ILE B  79  1  O  LEU B  76   N  ALA B   9           
SHEET    5  BA 7 HIS B 107  SER B 112  1  O  HIS B 107   N  ALA B  77           
SHEET    6  BA 7 SER B 145  ALA B 150  1  O  THR B 146   N  TYR B 110           
SHEET    7  BA 7 ARG B 215  LEU B 218  1  O  ILE B 216   N  TYR B 149           
SHEET    1  BB 3 ILE B 152  TYR B 153  0                                        
SHEET    2  BB 3 LEU B 187  LEU B 190  1  O  PRO B 188   N  ILE B 152           
SHEET    3  BB 3 GLU B 221  LEU B 223 -1  O  GLU B 221   N  TRP B 189           
SHEET    1  BC 3 MET B 167  LEU B 169  0                                        
SHEET    2  BC 3 PHE B 175  ALA B 179 -1  O  GLU B 176   N  GLU B 168           
SHEET    3  BC 3 VAL B 240  GLN B 244  1  O  THR B 241   N  TRP B 177           
SHEET    1  CA 7 VAL C  53  GLN C  57  0                                        
SHEET    2  CA 7 HIS C  31  VAL C  36  1  O  VAL C  32   N  THR C  54           
SHEET    3  CA 7 THR C   7  VAL C  10  1  O  ILE C   8   N  ARG C  33           
SHEET    4  CA 7 LEU C  76  ILE C  79  1  O  LEU C  76   N  ALA C   9           
SHEET    5  CA 7 HIS C 107  SER C 112  1  O  HIS C 107   N  ALA C  77           
SHEET    6  CA 7 SER C 145  ALA C 150  1  O  THR C 146   N  TYR C 110           
SHEET    7  CA 7 ARG C 215  LEU C 218  1  O  ILE C 216   N  TYR C 149           
SHEET    1  CB 3 ILE C 152  TYR C 153  0                                        
SHEET    2  CB 3 LEU C 187  LEU C 190  1  O  PRO C 188   N  ILE C 152           
SHEET    3  CB 3 GLU C 221  LEU C 223 -1  O  GLU C 221   N  TRP C 189           
SHEET    1  CC 3 GLU C 168  LEU C 169  0                                        
SHEET    2  CC 3 PHE C 175  ALA C 179 -1  O  GLU C 176   N  GLU C 168           
SHEET    3  CC 3 VAL C 240  GLN C 244  1  O  THR C 241   N  TRP C 177           
SHEET    1  DA 7 VAL D  53  GLN D  57  0                                        
SHEET    2  DA 7 VAL D  32  VAL D  36  1  O  VAL D  32   N  THR D  54           
SHEET    3  DA 7 ILE D   8  VAL D  10  1  O  ILE D   8   N  ARG D  33           
SHEET    4  DA 7 LEU D  76  ILE D  79  1  O  LEU D  76   N  ALA D   9           
SHEET    5  DA 7 HIS D 107  SER D 112  1  O  HIS D 107   N  ALA D  77           
SHEET    6  DA 7 SER D 145  ALA D 150  1  O  THR D 146   N  TYR D 110           
SHEET    7  DA 7 ARG D 215  LEU D 218  1  O  ILE D 216   N  TYR D 149           
SHEET    1  DB 3 ILE D 152  TYR D 153  0                                        
SHEET    2  DB 3 LEU D 187  LEU D 190  1  O  PRO D 188   N  ILE D 152           
SHEET    3  DB 3 GLU D 221  LEU D 223 -1  O  GLU D 221   N  TRP D 189           
SHEET    1  DC 3 MET D 167  LEU D 169  0                                        
SHEET    2  DC 3 PHE D 175  ALA D 179 -1  O  GLU D 176   N  GLU D 168           
SHEET    3  DC 3 VAL D 240  GLN D 244  1  O  THR D 241   N  TRP D 177           
SHEET    1  EA 7 VAL E  53  GLN E  57  0                                        
SHEET    2  EA 7 VAL E  32  VAL E  36  1  O  VAL E  32   N  THR E  54           
SHEET    3  EA 7 ILE E   8  VAL E  10  1  O  ILE E   8   N  ARG E  33           
SHEET    4  EA 7 LEU E  76  ILE E  79  1  O  LEU E  76   N  ALA E   9           
SHEET    5  EA 7 HIS E 107  SER E 112  1  O  HIS E 107   N  ALA E  77           
SHEET    6  EA 7 SER E 145  ALA E 150  1  O  THR E 146   N  TYR E 110           
SHEET    7  EA 7 ARG E 215  LEU E 218  1  O  ILE E 216   N  TYR E 149           
SHEET    1  EB 3 ILE E 152  TYR E 153  0                                        
SHEET    2  EB 3 LEU E 187  LEU E 190  1  O  PRO E 188   N  ILE E 152           
SHEET    3  EB 3 GLU E 221  LEU E 223 -1  O  GLU E 221   N  TRP E 189           
SHEET    1  EC 3 MET E 167  LEU E 169  0                                        
SHEET    2  EC 3 PHE E 175  ALA E 179 -1  O  GLU E 176   N  GLU E 168           
SHEET    3  EC 3 VAL E 240  GLN E 244  1  O  THR E 241   N  TRP E 177           
SHEET    1  FA 7 VAL F  53  GLN F  57  0                                        
SHEET    2  FA 7 VAL F  32  VAL F  36  1  O  VAL F  32   N  THR F  54           
SHEET    3  FA 7 ILE F   8  VAL F  10  1  O  ILE F   8   N  ARG F  33           
SHEET    4  FA 7 LEU F  76  ILE F  79  1  O  LEU F  76   N  ALA F   9           
SHEET    5  FA 7 HIS F 107  SER F 111  1  O  HIS F 107   N  ALA F  77           
SHEET    6  FA 7 SER F 145  ALA F 150  1  O  THR F 146   N  TYR F 110           
SHEET    7  FA 7 ARG F 215  LEU F 218  1  O  ILE F 216   N  TYR F 149           
SHEET    1  FB 3 ILE F 152  TYR F 153  0                                        
SHEET    2  FB 3 LEU F 187  LEU F 190  1  O  PRO F 188   N  ILE F 152           
SHEET    3  FB 3 GLU F 221  LEU F 223 -1  O  GLU F 221   N  TRP F 189           
SHEET    1  FC 3 GLU F 168  LEU F 169  0                                        
SHEET    2  FC 3 PHE F 175  ALA F 179 -1  O  GLU F 176   N  GLU F 168           
SHEET    3  FC 3 VAL F 240  GLN F 244  1  O  THR F 241   N  TRP F 177           
SHEET    1  GA 7 VAL G  53  GLN G  57  0                                        
SHEET    2  GA 7 HIS G  31  VAL G  36  1  O  VAL G  32   N  THR G  54           
SHEET    3  GA 7 THR G   7  VAL G  10  1  O  ILE G   8   N  ARG G  33           
SHEET    4  GA 7 LEU G  76  ILE G  79  1  O  LEU G  76   N  ALA G   9           
SHEET    5  GA 7 HIS G 107  SER G 112  1  O  HIS G 107   N  ALA G  77           
SHEET    6  GA 7 SER G 145  ALA G 150  1  O  THR G 146   N  TYR G 110           
SHEET    7  GA 7 HIS G 214  LEU G 218  1  O  HIS G 214   N  PHE G 147           
SHEET    1  GB 3 ILE G 152  TYR G 153  0                                        
SHEET    2  GB 3 LEU G 187  LEU G 190  1  O  PRO G 188   N  ILE G 152           
SHEET    3  GB 3 GLU G 221  LEU G 223 -1  O  GLU G 221   N  TRP G 189           
SHEET    1  GC 3 MET G 167  LEU G 169  0                                        
SHEET    2  GC 3 PHE G 175  ALA G 179 -1  O  GLU G 176   N  GLU G 168           
SHEET    3  GC 3 VAL G 240  GLN G 244  1  O  THR G 241   N  TRP G 177           
SHEET    1  HA 7 VAL H  53  GLN H  57  0                                        
SHEET    2  HA 7 VAL H  32  VAL H  36  1  O  VAL H  32   N  THR H  54           
SHEET    3  HA 7 ILE H   8  VAL H  10  1  O  ILE H   8   N  ARG H  33           
SHEET    4  HA 7 LEU H  76  ILE H  79  1  O  LEU H  76   N  ALA H   9           
SHEET    5  HA 7 HIS H 107  SER H 112  1  O  HIS H 107   N  ALA H  77           
SHEET    6  HA 7 SER H 145  ALA H 150  1  O  THR H 146   N  TYR H 110           
SHEET    7  HA 7 ARG H 215  LEU H 218  1  O  ILE H 216   N  TYR H 149           
SHEET    1  HB 3 ILE H 152  TYR H 153  0                                        
SHEET    2  HB 3 LEU H 187  LEU H 190  1  O  PRO H 188   N  ILE H 152           
SHEET    3  HB 3 GLU H 221  LEU H 223 -1  O  GLU H 221   N  TRP H 189           
SHEET    1  HC 3 GLU H 168  LEU H 169  0                                        
SHEET    2  HC 3 PHE H 175  ALA H 179 -1  O  GLU H 176   N  GLU H 168           
SHEET    3  HC 3 VAL H 240  GLN H 244  1  O  THR H 241   N  TRP H 177           
SHEET    1  IA 2 ARG I 685  ARG I 686  0                                        
SHEET    2  IA 2 PRO I 692  LEU I 693 -1  O  LEU I 693   N  ARG I 685           
SHEET    1  JA 2 TRP J 684  ARG J 686  0                                        
SHEET    2  JA 2 PRO J 692  CYS J 694 -1  O  LEU J 693   N  ARG J 685           
SHEET    1  KA 2 TRP K 684  ARG K 686  0                                        
SHEET    2  KA 2 PRO K 692  CYS K 694 -1  O  LEU K 693   N  ARG K 685           
SHEET    1  LA 2 ARG L 685  ARG L 686  0                                        
SHEET    2  LA 2 PRO L 692  LEU L 693 -1  O  LEU L 693   N  ARG L 685           
SHEET    1  MA 2 ARG M 684  ARG M 685  0                                        
SHEET    2  MA 2 PRO M 691  LEU M 692 -1  O  LEU M 692   N  ARG M 684           
SHEET    1  NA 2 TRP N 684  ARG N 686  0                                        
SHEET    2  NA 2 PRO N 692  CYS N 694 -1  O  LEU N 693   N  ARG N 685           
SHEET    1  OA 2 TRP O 684  ARG O 686  0                                        
SHEET    2  OA 2 PRO O 692  CYS O 694 -1  O  LEU O 693   N  ARG O 685           
SHEET    1  PA 2 ARG P 685  ARG P 686  0                                        
SHEET    2  PA 2 PRO P 692  LEU P 693 -1  O  LEU P 693   N  ARG P 685           
LINK        ZN    ZN I1713                 SG  CYS I 673     1555   1555  2.40  
LINK        ZN    ZN I1713                 SG  CYS I 697     1555   1555  2.43  
LINK        ZN    ZN I1713                 SG  CYS I 676     1555   1555  2.11  
LINK        ZN    ZN I1713                 SG  CYS I 694     1555   1555  2.25  
LINK        ZN    ZN J1713                 SG  CYS J 673     1555   1555  2.50  
LINK        ZN    ZN J1713                 SG  CYS J 694     1555   1555  2.28  
LINK        ZN    ZN J1713                 SG  CYS J 697     1555   1555  2.46  
LINK        ZN    ZN J1713                 SG  CYS J 676     1555   1555  2.07  
LINK        ZN    ZN K1712                 SG  CYS K 676     1555   1555  2.31  
LINK        ZN    ZN K1712                 SG  CYS K 694     1555   1555  2.17  
LINK        ZN    ZN K1712                 SG  CYS K 673     1555   1555  2.40  
LINK        ZN    ZN K1712                 SG  CYS K 697     1555   1555  2.44  
LINK        ZN    ZN L1713                 SG  CYS L 694     1555   1555  2.22  
LINK        ZN    ZN L1713                 SG  CYS L 673     1555   1555  2.40  
LINK        ZN    ZN L1713                 SG  CYS L 676     1555   1555  2.37  
LINK        ZN    ZN L1713                 SG  CYS L 697     1555   1555  2.35  
LINK        ZN    ZN M1713                 SG  CYS M 693     1555   1555  2.17  
LINK        ZN    ZN M1713                 SG  CYS M 696     1555   1555  2.18  
LINK        ZN    ZN M1713                 SG  CYS M 675     1555   1555  2.18  
LINK        ZN    ZN M1713                 SG  CYS M 672     1555   1555  2.42  
LINK        ZN    ZN N1713                 SG  CYS N 676     1555   1555  2.12  
LINK        ZN    ZN N1713                 SG  CYS N 694     1555   1555  2.29  
LINK        ZN    ZN N1713                 SG  CYS N 697     1555   1555  2.44  
LINK        ZN    ZN N1713                 SG  CYS N 673     1555   1555  2.44  
LINK        ZN    ZN O1712                 SG  CYS O 676     1555   1555  2.12  
LINK        ZN    ZN O1712                 SG  CYS O 694     1555   1555  2.22  
LINK        ZN    ZN O1712                 SG  CYS O 697     1555   1555  2.31  
LINK        ZN    ZN O1712                 SG  CYS O 673     1555   1555  2.36  
LINK        ZN    ZN P1713                 SG  CYS P 694     1555   1555  2.17  
LINK        ZN    ZN P1713                 SG  CYS P 697     1555   1555  2.26  
LINK        ZN    ZN P1713                 SG  CYS P 676     1555   1555  2.03  
LINK        ZN    ZN P1713                 SG  CYS P 673     1555   1555  2.34  
SITE     1 AC1 26 ASN A  12  THR A  14  GLY A  15  ARG A  16                    
SITE     2 AC1 26 GLN A  17  HIS A  37  ASN A  80  THR A  81                    
SITE     3 AC1 26 THR A  82  GLN A  84  ALA A  85  MET A 127                    
SITE     4 AC1 26 TRP A 128  LYS A 131  ALA A 150  GLY A 151                    
SITE     5 AC1 26 ILE A 152  TYR A 153  ASN A 156  TYR A 276                    
SITE     6 AC1 26 HOH A2020  HOH A2044  HOH A2047  HOH A2082                    
SITE     7 AC1 26 HOH A2177  HOH A2179                                          
SITE     1 AC2  5 HIS C 194  ARG C 329  CYS K 676  ARG K 708                    
SITE     2 AC2  5 LEU K 710                                                     
SITE     1 AC3  5 HIS E 194  ARG E 329  CYS M 675  ARG M 707                    
SITE     2 AC3  5 LEU M 709                                                     
SITE     1 AC4  5 HIS G 194  ARG G 329  HOH G2233  ARG O 708                    
SITE     2 AC4  5 LEU O 710                                                     
SITE     1 AC5  4 ASN A  12  THR A  14  VAL A  36  HIS A  37                    
SITE     1 AC6  4 ASN C  12  THR C  14  VAL C  36  HIS C  37                    
SITE     1 AC7  4 ASN D  12  THR D  14  VAL D  36  HIS D  37                    
SITE     1 AC8  3 ASN E  12  ALA E  13  THR E  14                               
SITE     1 AC9  4 ASN F  12  ALA F  13  THR F  14  HIS F  37                    
SITE     1 BC1  5 ASN G  12  ALA G  13  THR G  14  VAL G  36                    
SITE     2 BC1  5 HIS G  37                                                     
SITE     1 BC2  5 ASN H  12  ALA H  13  THR H  14  VAL H  36                    
SITE     2 BC2  5 HIS H  37                                                     
SITE     1 BC3 21 ASN B  12  THR B  14  GLY B  15  ARG B  16                    
SITE     2 BC3 21 GLN B  17  HIS B  37  ASN B  80  THR B  81                    
SITE     3 BC3 21 THR B  82  GLN B  84  MET B 127  TRP B 128                    
SITE     4 BC3 21 LYS B 131  ALA B 150  GLY B 151  ILE B 152                    
SITE     5 BC3 21 TYR B 153  ASN B 156  TYR B 276  HOH B2014                    
SITE     6 BC3 21 HOH B2190                                                     
SITE     1 BC4 23 ASN C  12  THR C  14  GLY C  15  ARG C  16                    
SITE     2 BC4 23 GLN C  17  HIS C  37  ASN C  80  THR C  81                    
SITE     3 BC4 23 GLN C  84  ALA C  85  MET C 127  TRP C 128                    
SITE     4 BC4 23 LYS C 131  ALA C 150  GLY C 151  ILE C 152                    
SITE     5 BC4 23 TYR C 153  ASN C 156  TYR C 276  HOH C2016                    
SITE     6 BC4 23 HOH C2110  HOH C2228  HOH C2229                               
SITE     1 BC5 23 ASN D  12  THR D  14  GLY D  15  ARG D  16                    
SITE     2 BC5 23 GLN D  17  HIS D  37  ASN D  80  THR D  81                    
SITE     3 BC5 23 THR D  82  ALA D  85  MET D 113  MET D 127                    
SITE     4 BC5 23 TRP D 128  LYS D 131  ALA D 150  GLY D 151                    
SITE     5 BC5 23 ILE D 152  TYR D 153  ASN D 156  TYR D 276                    
SITE     6 BC5 23 HOH D2009  HOH D2210  HOH D2211                               
SITE     1 BC6 25 ASN E  12  THR E  14  GLY E  15  ARG E  16                    
SITE     2 BC6 25 GLN E  17  HIS E  37  ASN E  80  THR E  81                    
SITE     3 BC6 25 THR E  82  GLN E  84  MET E 113  MET E 127                    
SITE     4 BC6 25 TRP E 128  LYS E 131  ALA E 150  GLY E 151                    
SITE     5 BC6 25 ILE E 152  TYR E 153  ASN E 156  TYR E 276                    
SITE     6 BC6 25 HOH E2017  HOH E2070  HOH E2115  HOH E2240                    
SITE     7 BC6 25 HOH E2241                                                     
SITE     1 BC7 24 ASN F  12  THR F  14  GLY F  15  ARG F  16                    
SITE     2 BC7 24 GLN F  17  HIS F  37  ASN F  80  THR F  81                    
SITE     3 BC7 24 THR F  82  ALA F  85  MET F 113  MET F 127                    
SITE     4 BC7 24 LYS F 131  ALA F 150  GLY F 151  ILE F 152                    
SITE     5 BC7 24 TYR F 153  ASN F 156  TYR F 276  HOH F2093                    
SITE     6 BC7 24 HOH F2240  HOH F2241  HOH F2243  HOH F2244                    
SITE     1 BC8 23 ASN G  12  THR G  14  GLY G  15  ARG G  16                    
SITE     2 BC8 23 GLN G  17  HIS G  37  ASN G  80  THR G  81                    
SITE     3 BC8 23 THR G  82  ALA G  85  MET G 127  TRP G 128                    
SITE     4 BC8 23 LYS G 131  ALA G 150  GLY G 151  ILE G 152                    
SITE     5 BC8 23 TYR G 153  ASN G 156  TYR G 276  HOH G2122                    
SITE     6 BC8 23 HOH G2244  HOH G2245  HOH G2246                               
SITE     1 BC9 23 ASN H  12  THR H  14  GLY H  15  ARG H  16                    
SITE     2 BC9 23 GLN H  17  HIS H  37  ASN H  80  THR H  81                    
SITE     3 BC9 23 THR H  82  GLN H  84  ALA H  85  MET H 127                    
SITE     4 BC9 23 TRP H 128  LYS H 131  ALA H 150  GLY H 151                    
SITE     5 BC9 23 ILE H 152  TYR H 153  ASN H 156  TYR H 276                    
SITE     6 BC9 23 HOH H2206  HOH H2208  HOH H2209                               
SITE     1 CC1  4 CYS I 673  CYS I 676  CYS I 694  CYS I 697                    
SITE     1 CC2  4 CYS J 673  CYS J 676  CYS J 694  CYS J 697                    
SITE     1 CC3  4 CYS K 673  CYS K 676  CYS K 694  CYS K 697                    
SITE     1 CC4  4 CYS L 673  CYS L 676  CYS L 694  CYS L 697                    
SITE     1 CC5  4 CYS M 672  CYS M 675  CYS M 693  CYS M 696                    
SITE     1 CC6  4 CYS N 673  CYS N 676  CYS N 694  CYS N 697                    
SITE     1 CC7  4 CYS O 673  CYS O 676  CYS O 694  CYS O 697                    
SITE     1 CC8  4 CYS P 673  CYS P 676  CYS P 694  CYS P 697                    
CRYST1  227.520  227.520  222.570  90.00  90.00 120.00 H 3          72          
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      0.004395  0.002538  0.000000        0.00000                         
SCALE2      0.000000  0.005075  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004493        0.00000                         
MODEL        1                                                                  
ATOM      1  N   THR I 671     -21.540-106.246 190.248  1.00 70.21           N  
ATOM      2  CA  THR I 671     -22.830-106.886 190.479  1.00 66.47           C  
ATOM      3  C   THR I 671     -23.988-105.889 190.391  1.00 63.39           C  
ATOM      4  O   THR I 671     -23.946-104.949 189.596  1.00 68.73           O  
ATOM      5  CB  THR I 671     -22.860-107.576 191.851  1.00 66.88           C  
ATOM      6  OG1 THR I 671     -22.589-106.614 192.874  1.00 76.41           O  
ATOM      7  CG2 THR I 671     -21.813-108.679 191.914  1.00 76.64           C  
ATOM      8  N   THR I 672     -25.016-106.093 191.208  1.00 49.85           N  
ATOM      9  CA  THR I 672     -26.187-105.219 191.196  1.00 52.41           C  
ATOM     10  C   THR I 672     -27.111-105.490 192.384  1.00 49.16           C  
ATOM     11  O   THR I 672     -27.486-106.631 192.628  1.00 45.28           O  
ATOM     12  CB  THR I 672     -27.003-105.415 189.894  1.00 46.54           C  
ATOM     13  OG1 THR I 672     -26.259-104.908 188.780  1.00 68.29           O  
ATOM     14  CG2 THR I 672     -28.335-104.691 189.976  1.00 54.23           C  
ATOM     15  N   CYS I 673     -27.481-104.443 193.119  1.00 50.94           N  
ATOM     16  CA  CYS I 673     -28.371-104.621 194.264  1.00 46.97           C  
ATOM     17  C   CYS I 673     -29.692-105.167 193.756  1.00 37.46           C  
ATOM     18  O   CYS I 673     -30.179-104.752 192.712  1.00 36.04           O  
ATOM     19  CB  CYS I 673     -28.618-103.290 194.998  1.00 51.46           C  
ATOM     20  SG  CYS I 673     -29.761-103.390 196.441  1.00 30.68           S  
ATOM     21  N   THR I 674     -30.261-106.107 194.497  1.00 32.02           N  
ATOM     22  CA  THR I 674     -31.533-106.700 194.121  1.00 34.90           C  
ATOM     23  C   THR I 674     -32.635-105.698 194.408  1.00 35.06           C  
ATOM     24  O   THR I 674     -33.706-105.750 193.813  1.00 41.36           O  
ATOM     25  CB  THR I 674     -31.810-107.966 194.942  1.00 41.23           C  
ATOM     26  OG1 THR I 674     -30.737-108.896 194.760  1.00 39.22           O  
ATOM     27  CG2 THR I 674     -33.118-108.603 194.510  1.00 51.82           C  
ATOM     28  N   ASN I 675     -32.359-104.779 195.326  1.00 39.89           N  
ATOM     29  CA  ASN I 675     -33.340-103.779 195.713  1.00 38.91           C  
ATOM     30  C   ASN I 675     -33.330-102.505 194.871  1.00 32.22           C  
ATOM     31  O   ASN I 675     -34.188-102.317 194.009  1.00 41.60           O  
ATOM     32  CB  ASN I 675     -33.150-103.403 197.182  1.00 34.33           C  
ATOM     33  CG  ASN I 675     -34.310-102.602 197.721  1.00 35.52           C  
ATOM     34  OD1 ASN I 675     -34.131-101.657 198.490  1.00 28.97           O  
ATOM     35  ND2 ASN I 675     -35.516-102.981 197.320  1.00 25.80           N  
ATOM     36  N   CYS I 676     -32.362-101.630 195.131  1.00 31.06           N  
ATOM     37  CA  CYS I 676     -32.258-100.355 194.423  1.00 33.67           C  
ATOM     38  C   CYS I 676     -31.532-100.445 193.089  1.00 34.98           C  
ATOM     39  O   CYS I 676     -31.384 -99.443 192.389  1.00 33.60           O  
ATOM     40  CB  CYS I 676     -31.550 -99.334 195.299  1.00 28.98           C  
ATOM     41  SG  CYS I 676     -29.903 -99.862 195.712  1.00 26.63           S  
ATOM     42  N   PHE I 677     -31.058-101.639 192.755  1.00 32.27           N  
ATOM     43  CA  PHE I 677     -30.379-101.876 191.489  1.00 35.76           C  
ATOM     44  C   PHE I 677     -29.091-101.089 191.270  1.00 36.43           C  
ATOM     45  O   PHE I 677     -28.531-101.106 190.176  1.00 43.19           O  
ATOM     46  CB  PHE I 677     -31.349-101.597 190.344  1.00 33.74           C  
ATOM     47  CG  PHE I 677     -32.631-102.362 190.447  1.00 54.49           C  
ATOM     48  CD1 PHE I 677     -32.646-103.742 190.282  1.00 66.86           C  
ATOM     49  CD2 PHE I 677     -33.824-101.705 190.732  1.00 69.57           C  
ATOM     50  CE1 PHE I 677     -33.833-104.462 190.401  1.00 75.19           C  
ATOM     51  CE2 PHE I 677     -35.018-102.413 190.854  1.00 73.36           C  
ATOM     52  CZ  PHE I 677     -35.022-103.795 190.688  1.00 77.25           C  
ATOM     53  N   THR I 678     -28.616-100.395 192.297  1.00 31.61           N  
ATOM     54  CA  THR I 678     -27.378 -99.638 192.159  1.00 28.69           C  
ATOM     55  C   THR I 678     -26.243-100.611 191.866  1.00 34.90           C  
ATOM     56  O   THR I 678     -26.339-101.799 192.169  1.00 36.42           O  
ATOM     57  CB  THR I 678     -27.025 -98.863 193.454  1.00 40.97           C  
ATOM     58  OG1 THR I 678     -25.821 -98.113 193.243  1.00 38.04           O  
ATOM     59  CG2 THR I 678     -26.812 -99.828 194.631  1.00 17.15           C  
ATOM     60  N   GLN I 679     -25.173-100.104 191.267  1.00 39.82           N  
ATOM     61  CA  GLN I 679     -24.011-100.923 190.956  1.00 42.18           C  
ATOM     62  C   GLN I 679     -22.820-100.300 191.658  1.00 49.60           C  
ATOM     63  O   GLN I 679     -21.725-100.865 191.684  1.00 50.99           O  
ATOM     64  CB  GLN I 679     -23.753-100.946 189.453  1.00 44.56           C  
ATOM     65  CG  GLN I 679     -24.692-101.825 188.652  1.00 38.37           C  
ATOM     66  CD  GLN I 679     -24.346-101.809 187.175  1.00 57.72           C  
ATOM     67  OE1 GLN I 679     -23.196-102.042 186.794  1.00 56.90           O  
ATOM     68  NE2 GLN I 679     -25.336-101.531 186.336  1.00 70.88           N  
ATOM     69  N   THR I 680     -23.051 -99.122 192.226  1.00 49.94           N  
ATOM     70  CA  THR I 680     -22.018 -98.385 192.935  1.00 48.61           C  
ATOM     71  C   THR I 680     -22.298 -98.417 194.435  1.00 43.43           C  
ATOM     72  O   THR I 680     -23.314 -97.903 194.894  1.00 50.54           O  
ATOM     73  CB  THR I 680     -21.979 -96.920 192.456  1.00 51.63           C  
ATOM     74  OG1 THR I 680     -21.833 -96.894 191.032  1.00 45.55           O  
ATOM     75  CG2 THR I 680     -20.818 -96.172 193.087  1.00 53.64           C  
ATOM     76  N   THR I 681     -21.403 -99.038 195.194  1.00 39.72           N  
ATOM     77  CA  THR I 681     -21.565 -99.118 196.637  1.00 40.88           C  
ATOM     78  C   THR I 681     -20.243 -99.485 197.305  1.00 38.02           C  
ATOM     79  O   THR I 681     -19.454-100.254 196.759  1.00 40.62           O  
ATOM     80  CB  THR I 681     -22.651-100.150 197.026  1.00 35.76           C  
ATOM     81  OG1 THR I 681     -22.928-100.041 198.428  1.00 41.31           O  
ATOM     82  CG2 THR I 681     -22.191-101.565 196.714  1.00 35.68           C  
ATOM     83  N   PRO I 682     -19.983 -98.927 198.496  1.00 41.22           N  
ATOM     84  CA  PRO I 682     -18.748 -99.192 199.245  1.00 44.78           C  
ATOM     85  C   PRO I 682     -18.605-100.603 199.826  1.00 49.62           C  
ATOM     86  O   PRO I 682     -17.534-100.977 200.305  1.00 48.88           O  
ATOM     87  CB  PRO I 682     -18.777 -98.123 200.336  1.00 47.37           C  
ATOM     88  CG  PRO I 682     -20.244 -97.954 200.590  1.00 43.88           C  
ATOM     89  CD  PRO I 682     -20.815 -97.928 199.194  1.00 30.78           C  
ATOM     90  N   LEU I 683     -19.676-101.387 199.781  1.00 48.92           N  
ATOM     91  CA  LEU I 683     -19.638-102.737 200.334  1.00 50.81           C  
ATOM     92  C   LEU I 683     -20.895-103.499 199.938  1.00 53.51           C  
ATOM     93  O   LEU I 683     -21.999-102.958 200.010  1.00 62.22           O  
ATOM     94  CB  LEU I 683     -19.544-102.658 201.864  1.00 43.25           C  
ATOM     95  CG  LEU I 683     -19.631-103.927 202.718  1.00 61.54           C  
ATOM     96  CD1 LEU I 683     -18.320-104.696 202.657  1.00 60.32           C  
ATOM     97  CD2 LEU I 683     -19.933-103.538 204.156  1.00 53.95           C  
ATOM     98  N   TRP I 684     -20.736-104.746 199.506  1.00 44.14           N  
ATOM     99  CA  TRP I 684     -21.899-105.541 199.143  1.00 45.62           C  
ATOM    100  C   TRP I 684     -22.271-106.416 200.327  1.00 46.92           C  
ATOM    101  O   TRP I 684     -21.405-106.928 201.034  1.00 45.05           O  
ATOM    102  CB  TRP I 684     -21.628-106.409 197.908  1.00 45.45           C  
ATOM    103  CG  TRP I 684     -21.355-105.613 196.655  1.00 46.32           C  
ATOM    104  CD1 TRP I 684     -20.130-105.339 196.104  1.00 31.35           C  
ATOM    105  CD2 TRP I 684     -22.323-104.951 195.826  1.00 35.63           C  
ATOM    106  NE1 TRP I 684     -20.279-104.549 194.989  1.00 55.59           N  
ATOM    107  CE2 TRP I 684     -21.612-104.295 194.795  1.00 47.34           C  
ATOM    108  CE3 TRP I 684     -23.721-104.845 195.857  1.00 36.78           C  
ATOM    109  CZ2 TRP I 684     -22.255-103.542 193.801  1.00 37.97           C  
ATOM    110  CZ3 TRP I 684     -24.360-104.093 194.867  1.00 21.56           C  
ATOM    111  CH2 TRP I 684     -23.624-103.452 193.854  1.00 20.77           C  
ATOM    112  N   ARG I 685     -23.570-106.550 200.558  1.00 51.85           N  
ATOM    113  CA  ARG I 685     -24.082-107.359 201.651  1.00 53.57           C  
ATOM    114  C   ARG I 685     -24.973-108.424 201.038  1.00 56.27           C  
ATOM    115  O   ARG I 685     -25.105-108.495 199.816  1.00 54.40           O  
ATOM    116  CB  ARG I 685     -24.882-106.486 202.622  1.00 47.90           C  
ATOM    117  CG  ARG I 685     -24.026-105.501 203.410  1.00 50.11           C  
ATOM    118  CD  ARG I 685     -24.881-104.458 204.112  1.00 30.75           C  
ATOM    119  NE  ARG I 685     -24.096-103.584 204.978  1.00 43.65           N  
ATOM    120  CZ  ARG I 685     -23.609-103.944 206.162  1.00 58.99           C  
ATOM    121  NH1 ARG I 685     -23.827-105.170 206.625  1.00 64.19           N  
ATOM    122  NH2 ARG I 685     -22.912-103.079 206.889  1.00 50.43           N  
ATOM    123  N   ARG I 686     -25.586-109.252 201.873  1.00 66.47           N  
ATOM    124  CA  ARG I 686     -26.447-110.300 201.351  1.00 76.07           C  
ATOM    125  C   ARG I 686     -27.812-110.419 202.006  1.00 80.70           C  
ATOM    126  O   ARG I 686     -28.012-110.041 203.163  1.00 76.22           O  
ATOM    127  CB  ARG I 686     -25.738-111.655 201.421  1.00 74.65           C  
ATOM    128  CG  ARG I 686     -24.639-111.829 200.393  1.00 68.30           C  
ATOM    129  CD  ARG I 686     -24.120-113.249 200.401  1.00 81.41           C  
ATOM    130  NE  ARG I 686     -23.159-113.481 199.329  1.00102.18           N  
ATOM    131  CZ  ARG I 686     -22.601-114.659 199.070  1.00110.96           C  
ATOM    132  NH1 ARG I 686     -22.911-115.717 199.808  1.00116.21           N  
ATOM    133  NH2 ARG I 686     -21.736-114.780 198.071  1.00109.88           N  
ATOM    134  N   ASN I 687     -28.745-110.951 201.223  1.00 89.25           N  
ATOM    135  CA  ASN I 687     -30.120-111.186 201.639  1.00 96.27           C  
ATOM    136  C   ASN I 687     -30.108-112.574 202.279  1.00 99.88           C  
ATOM    137  O   ASN I 687     -29.356-113.449 201.845  1.00100.57           O  
ATOM    138  CB  ASN I 687     -31.026-111.192 200.401  1.00 93.68           C  
ATOM    139  CG  ASN I 687     -32.500-111.308 200.743  1.00105.05           C  
ATOM    140  OD1 ASN I 687     -33.272-111.911 199.997  1.00111.87           O  
ATOM    141  ND2 ASN I 687     -32.903-110.713 201.860  1.00107.71           N  
ATOM    142  N   PRO I 688     -30.916-112.790 203.332  1.00 99.55           N  
ATOM    143  CA  PRO I 688     -30.938-114.108 203.972  1.00 99.94           C  
ATOM    144  C   PRO I 688     -31.074-115.261 202.971  1.00102.03           C  
ATOM    145  O   PRO I 688     -30.777-116.413 203.292  1.00102.51           O  
ATOM    146  CB  PRO I 688     -32.127-113.996 204.915  1.00 96.25           C  
ATOM    147  CG  PRO I 688     -32.001-112.582 205.393  1.00 82.59           C  
ATOM    148  CD  PRO I 688     -31.709-111.820 204.113  1.00 91.05           C  
ATOM    149  N   GLU I 689     -31.513-114.940 201.757  1.00103.77           N  
ATOM    150  CA  GLU I 689     -31.682-115.934 200.702  1.00102.08           C  
ATOM    151  C   GLU I 689     -30.400-116.099 199.883  1.00 95.92           C  
ATOM    152  O   GLU I 689     -30.162-117.150 199.290  1.00 91.84           O  
ATOM    153  CB  GLU I 689     -32.838-115.522 199.782  1.00105.96           C  
ATOM    154  CG  GLU I 689     -33.087-116.474 198.623  1.00112.01           C  
ATOM    155  CD  GLU I 689     -34.272-116.056 197.772  1.00118.87           C  
ATOM    156  OE1 GLU I 689     -34.274-114.907 197.281  1.00121.81           O  
ATOM    157  OE2 GLU I 689     -35.199-116.876 197.592  1.00119.84           O  
ATOM    158  N   GLY I 690     -29.578-115.054 199.856  1.00 96.77           N  
ATOM    159  CA  GLY I 690     -28.333-115.104 199.110  1.00 94.05           C  
ATOM    160  C   GLY I 690     -28.213-113.978 198.099  1.00 90.54           C  
ATOM    161  O   GLY I 690     -27.163-113.803 197.475  1.00 86.16           O  
ATOM    162  N   GLN I 691     -29.290-113.212 197.942  1.00 87.08           N  
ATOM    163  CA  GLN I 691     -29.325-112.095 197.000  1.00 79.31           C  
ATOM    164  C   GLN I 691     -28.395-110.965 197.433  1.00 69.68           C  
ATOM    165  O   GLN I 691     -28.310-110.635 198.617  1.00 71.62           O  
ATOM    166  CB  GLN I 691     -30.752-111.556 196.876  1.00 80.41           C  
ATOM    167  CG  GLN I 691     -31.787-112.607 196.513  1.00 87.00           C  
ATOM    168  CD  GLN I 691     -33.174-112.021 196.347  1.00 87.86           C  
ATOM    169  OE1 GLN I 691     -33.718-111.413 197.269  1.00 98.40           O  
ATOM    170  NE2 GLN I 691     -33.754-112.201 195.167  1.00 84.15           N  
ATOM    171  N   PRO I 692     -27.686-110.353 196.473  1.00 56.59           N  
ATOM    172  CA  PRO I 692     -26.764-109.256 196.782  1.00 52.71           C  
ATOM    173  C   PRO I 692     -27.461-107.904 196.937  1.00 43.42           C  
ATOM    174  O   PRO I 692     -28.185-107.458 196.046  1.00 36.03           O  
ATOM    175  CB  PRO I 692     -25.808-109.277 195.598  1.00 51.60           C  
ATOM    176  CG  PRO I 692     -26.728-109.632 194.466  1.00 59.45           C  
ATOM    177  CD  PRO I 692     -27.591-110.738 195.053  1.00 53.42           C  
ATOM    178  N   LEU I 693     -27.239-107.259 198.076  1.00 36.20           N  
ATOM    179  CA  LEU I 693     -27.824-105.952 198.345  1.00 36.99           C  
ATOM    180  C   LEU I 693     -26.690-104.964 198.608  1.00 32.29           C  
ATOM    181  O   LEU I 693     -25.647-105.342 199.131  1.00 35.67           O  
ATOM    182  CB  LEU I 693     -28.746-106.028 199.564  1.00 28.93           C  
ATOM    183  CG  LEU I 693     -29.907-107.027 199.483  1.00 26.34           C  
ATOM    184  CD1 LEU I 693     -30.592-107.123 200.844  1.00 42.86           C  
ATOM    185  CD2 LEU I 693     -30.900-106.601 198.414  1.00 31.68           C  
ATOM    186  N   CYS I 694     -26.878-103.702 198.241  1.00 34.11           N  
ATOM    187  CA  CYS I 694     -25.828-102.721 198.477  1.00 23.02           C  
ATOM    188  C   CYS I 694     -25.717-102.469 199.975  1.00 26.60           C  
ATOM    189  O   CYS I 694     -26.484-103.012 200.764  1.00 29.73           O  
ATOM    190  CB  CYS I 694     -26.127-101.412 197.743  1.00 24.34           C  
ATOM    191  SG  CYS I 694     -27.535-100.496 198.377  1.00 28.96           S  
ATOM    192  N   ASN I 695     -24.759-101.643 200.365  1.00 30.72           N  
ATOM    193  CA  ASN I 695     -24.556-101.341 201.769  1.00 30.77           C  
ATOM    194  C   ASN I 695     -25.820-100.771 202.425  1.00 31.63           C  
ATOM    195  O   ASN I 695     -26.310-101.319 203.420  1.00 31.57           O  
ATOM    196  CB  ASN I 695     -23.390-100.361 201.917  1.00 26.07           C  
ATOM    197  CG  ASN I 695     -22.921-100.224 203.346  1.00 23.01           C  
ATOM    198  OD1 ASN I 695     -22.695-101.222 204.035  1.00 34.60           O  
ATOM    199  ND2 ASN I 695     -22.755 -98.986 203.799  1.00 26.78           N  
ATOM    200  N   ALA I 696     -26.347 -99.685 201.864  1.00 23.31           N  
ATOM    201  CA  ALA I 696     -27.541 -99.043 202.414  1.00 30.91           C  
ATOM    202  C   ALA I 696     -28.721-100.002 202.578  1.00 30.57           C  
ATOM    203  O   ALA I 696     -29.244-100.177 203.683  1.00 35.37           O  
ATOM    204  CB  ALA I 696     -27.951 -97.853 201.542  1.00 26.27           C  
ATOM    205  N   CYS I 697     -29.139-100.620 201.481  1.00 21.83           N  
ATOM    206  CA  CYS I 697     -30.255-101.554 201.523  1.00 25.99           C  
ATOM    207  C   CYS I 697     -30.015-102.705 202.505  1.00 27.68           C  
ATOM    208  O   CYS I 697     -30.897-103.046 203.297  1.00 26.79           O  
ATOM    209  CB  CYS I 697     -30.530-102.096 200.116  1.00 19.41           C  
ATOM    210  SG  CYS I 697     -31.098-100.818 198.943  1.00 22.77           S  
ATOM    211  N   GLY I 698     -28.820-103.290 202.459  1.00 22.40           N  
ATOM    212  CA  GLY I 698     -28.496-104.386 203.355  1.00 15.33           C  
ATOM    213  C   GLY I 698     -28.509-103.949 204.807  1.00 21.42           C  
ATOM    214  O   GLY I 698     -29.116-104.600 205.667  1.00 20.17           O  
ATOM    215  N   LEU I 699     -27.854-102.824 205.080  1.00 20.42           N  
ATOM    216  CA  LEU I 699     -27.782-102.292 206.436  1.00 15.24           C  
ATOM    217  C   LEU I 699     -29.163-101.856 206.930  1.00 23.65           C  
ATOM    218  O   LEU I 699     -29.504-102.057 208.095  1.00 22.17           O  
ATOM    219  CB  LEU I 699     -26.810-101.110 206.473  1.00 14.14           C  
ATOM    220  CG  LEU I 699     -26.580-100.379 207.797  1.00 31.68           C  
ATOM    221  CD1 LEU I 699     -26.120-101.365 208.862  1.00 34.36           C  
ATOM    222  CD2 LEU I 699     -25.543 -99.282 207.601  1.00 24.92           C  
ATOM    223  N   PHE I 700     -29.955-101.266 206.040  1.00 19.99           N  
ATOM    224  CA  PHE I 700     -31.283-100.801 206.406  1.00 18.53           C  
ATOM    225  C   PHE I 700     -32.160-101.977 206.828  1.00 20.97           C  
ATOM    226  O   PHE I 700     -32.723-101.972 207.924  1.00 23.47           O  
ATOM    227  CB  PHE I 700     -31.917-100.034 205.235  1.00 27.56           C  
ATOM    228  CG  PHE I 700     -33.228 -99.356 205.574  1.00 36.44           C  
ATOM    229  CD1 PHE I 700     -34.433-100.055 205.512  1.00 22.96           C  
ATOM    230  CD2 PHE I 700     -33.257 -98.014 205.948  1.00 24.26           C  
ATOM    231  CE1 PHE I 700     -35.645 -99.425 205.817  1.00 22.96           C  
ATOM    232  CE2 PHE I 700     -34.463 -97.379 206.254  1.00 16.82           C  
ATOM    233  CZ  PHE I 700     -35.657 -98.086 206.187  1.00 20.66           C  
ATOM    234  N   LEU I 701     -32.271-102.986 205.972  1.00 17.97           N  
ATOM    235  CA  LEU I 701     -33.077-104.155 206.298  1.00 17.98           C  
ATOM    236  C   LEU I 701     -32.660-104.758 207.645  1.00 26.49           C  
ATOM    237  O   LEU I 701     -33.508-105.102 208.476  1.00 24.82           O  
ATOM    238  CB  LEU I 701     -32.939-105.203 205.194  1.00 29.12           C  
ATOM    239  CG  LEU I 701     -33.520-106.594 205.459  1.00 30.49           C  
ATOM    240  CD1 LEU I 701     -35.019-106.513 205.694  1.00 32.10           C  
ATOM    241  CD2 LEU I 701     -33.215-107.483 204.274  1.00 30.06           C  
ATOM    242  N   LYS I 702     -31.354-104.864 207.871  1.00 22.04           N  
ATOM    243  CA  LYS I 702     -30.846-105.432 209.115  1.00 26.10           C  
ATOM    244  C   LYS I 702     -31.241-104.613 210.346  1.00 35.99           C  
ATOM    245  O   LYS I 702     -31.543-105.169 211.406  1.00 33.66           O  
ATOM    246  CB  LYS I 702     -29.324-105.540 209.056  1.00 32.21           C  
ATOM    247  CG  LYS I 702     -28.715-106.451 210.100  1.00 42.66           C  
ATOM    248  CD  LYS I 702     -27.198-106.491 209.958  1.00 61.62           C  
ATOM    249  CE  LYS I 702     -26.594-107.747 210.591  1.00 79.68           C  
ATOM    250  NZ  LYS I 702     -26.932-109.004 209.847  1.00 70.21           N  
ATOM    251  N   LEU I 703     -31.238-103.291 210.208  1.00 26.07           N  
ATOM    252  CA  LEU I 703     -31.574-102.428 211.331  1.00 27.77           C  
ATOM    253  C   LEU I 703     -33.065-102.246 211.585  1.00 23.27           C  
ATOM    254  O   LEU I 703     -33.499-102.228 212.728  1.00 20.95           O  
ATOM    255  CB  LEU I 703     -30.931-101.046 211.151  1.00 21.63           C  
ATOM    256  CG  LEU I 703     -29.408-100.902 211.332  1.00 45.46           C  
ATOM    257  CD1 LEU I 703     -28.963 -99.494 210.935  1.00 25.11           C  
ATOM    258  CD2 LEU I 703     -29.029-101.185 212.786  1.00 31.39           C  
ATOM    259  N   HIS I 704     -33.850-102.130 210.523  1.00 20.10           N  
ATOM    260  CA  HIS I 704     -35.274-101.884 210.685  1.00 21.42           C  
ATOM    261  C   HIS I 704     -36.215-103.034 210.372  1.00 18.16           C  
ATOM    262  O   HIS I 704     -37.386-102.952 210.690  1.00 14.03           O  
ATOM    263  CB  HIS I 704     -35.655-100.649 209.872  1.00 21.50           C  
ATOM    264  CG  HIS I 704     -34.782 -99.466 210.151  1.00 19.90           C  
ATOM    265  ND1 HIS I 704     -34.799 -98.799 211.356  1.00 19.88           N  
ATOM    266  CD2 HIS I 704     -33.830 -98.864 209.400  1.00 18.62           C  
ATOM    267  CE1 HIS I 704     -33.895 -97.837 211.336  1.00 30.67           C  
ATOM    268  NE2 HIS I 704     -33.292 -97.855 210.161  1.00 15.61           N  
ATOM    269  N   GLY I 705     -35.711-104.093 209.748  1.00 18.73           N  
ATOM    270  CA  GLY I 705     -36.556-105.240 209.467  1.00 18.91           C  
ATOM    271  C   GLY I 705     -37.228-105.348 208.114  1.00 17.53           C  
ATOM    272  O   GLY I 705     -37.654-106.437 207.740  1.00 23.21           O  
ATOM    273  N   VAL I 706     -37.329-104.243 207.378  1.00 18.71           N  
ATOM    274  CA  VAL I 706     -37.968-104.271 206.065  1.00 18.20           C  
ATOM    275  C   VAL I 706     -37.056-103.735 204.965  1.00 27.37           C  
ATOM    276  O   VAL I 706     -36.074-103.039 205.245  1.00 24.33           O  
ATOM    277  CB  VAL I 706     -39.262-103.442 206.065  1.00 29.92           C  
ATOM    278  CG1 VAL I 706     -40.259-104.031 207.052  1.00 29.05           C  
ATOM    279  CG2 VAL I 706     -38.943-102.003 206.433  1.00 17.25           C  
ATOM    280  N   VAL I 707     -37.390-104.049 203.712  1.00 18.98           N  
ATOM    281  CA  VAL I 707     -36.589-103.595 202.584  1.00 15.89           C  
ATOM    282  C   VAL I 707     -36.610-102.082 202.525  1.00 19.94           C  
ATOM    283  O   VAL I 707     -37.621-101.450 202.835  1.00 17.65           O  
ATOM    284  CB  VAL I 707     -37.117-104.126 201.226  1.00 25.59           C  
ATOM    285  CG1 VAL I 707     -37.371-105.622 201.307  1.00 26.42           C  
ATOM    286  CG2 VAL I 707     -38.368-103.385 200.827  1.00 31.42           C  
ATOM    287  N   ARG I 708     -35.488-101.505 202.122  1.00 16.02           N  
ATOM    288  CA  ARG I 708     -35.388-100.064 202.015  1.00 22.36           C  
ATOM    289  C   ARG I 708     -36.322 -99.573 200.905  1.00 27.37           C  
ATOM    290  O   ARG I 708     -36.166 -99.940 199.740  1.00 34.02           O  
ATOM    291  CB  ARG I 708     -33.941 -99.678 201.706  1.00 25.42           C  
ATOM    292  CG  ARG I 708     -33.641 -98.190 201.838  1.00 28.11           C  
ATOM    293  CD  ARG I 708     -32.132 -97.957 201.946  1.00 19.07           C  
ATOM    294  NE  ARG I 708     -31.437 -98.256 200.700  1.00 28.79           N  
ATOM    295  CZ  ARG I 708     -31.407 -97.442 199.651  1.00 38.96           C  
ATOM    296  NH1 ARG I 708     -32.030 -96.270 199.697  1.00 38.10           N  
ATOM    297  NH2 ARG I 708     -30.757 -97.801 198.557  1.00 34.14           N  
ATOM    298  N   PRO I 709     -37.323 -98.755 201.258  1.00 25.53           N  
ATOM    299  CA  PRO I 709     -38.273 -98.221 200.275  1.00 30.13           C  
ATOM    300  C   PRO I 709     -37.628 -97.167 199.378  1.00 31.16           C  
ATOM    301  O   PRO I 709     -36.786 -96.397 199.826  1.00 31.40           O  
ATOM    302  CB  PRO I 709     -39.373 -97.630 201.147  1.00 19.53           C  
ATOM    303  CG  PRO I 709     -38.616 -97.157 202.341  1.00 19.33           C  
ATOM    304  CD  PRO I 709     -37.685 -98.322 202.617  1.00 33.08           C  
ATOM    305  N   LEU I 710     -38.034 -97.140 198.112  1.00 41.13           N  
ATOM    306  CA  LEU I 710     -37.500 -96.189 197.142  1.00 44.89           C  
ATOM    307  C   LEU I 710     -38.618 -95.268 196.662  1.00 46.24           C  
ATOM    308  O   LEU I 710     -39.791 -95.631 196.740  1.00 44.87           O  
ATOM    309  CB  LEU I 710     -36.902 -96.959 195.967  1.00 53.09           C  
ATOM    310  CG  LEU I 710     -35.918 -98.049 196.404  1.00 49.62           C  
ATOM    311  CD1 LEU I 710     -35.454 -98.850 195.200  1.00 41.12           C  
ATOM    312  CD2 LEU I 710     -34.739 -97.407 197.115  1.00 30.73           C  
ATOM    313  N   SER I 711     -38.263 -94.086 196.163  1.00 54.38           N  
ATOM    314  CA  SER I 711     -39.271 -93.126 195.699  1.00 61.93           C  
ATOM    315  C   SER I 711     -39.914 -93.472 194.351  1.00 65.39           C  
ATOM    316  O   SER I 711     -39.515 -94.431 193.690  1.00 71.10           O  
ATOM    317  CB  SER I 711     -38.671 -91.713 195.643  1.00 53.05           C  
ATOM    318  OG  SER I 711     -37.552 -91.652 194.776  1.00 55.01           O  
ATOM    319  N   LEU I 712     -40.913 -92.675 193.969  1.00 71.45           N  
ATOM    320  CA  LEU I 712     -41.672 -92.830 192.720  1.00 74.87           C  
ATOM    321  C   LEU I 712     -42.890 -93.733 192.900  1.00 73.51           C  
ATOM    322  O   LEU I 712     -44.025 -93.318 192.650  1.00 70.82           O  
ATOM    323  CB  LEU I 712     -40.791 -93.383 191.588  1.00 72.37           C  
ATOM    324  CG  LEU I 712     -39.653 -92.493 191.081  1.00 65.53           C  
ATOM    325  CD1 LEU I 712     -38.839 -93.245 190.041  1.00 63.14           C  
ATOM    326  CD2 LEU I 712     -40.226 -91.213 190.496  1.00 67.34           C  
TER     327      LEU I 712                                                      
HETATM  328 ZN    ZN I1713     -29.370-101.174 197.276  1.00 32.45          ZN  
HETATM  329  O   HOH I2001     -16.785-107.670 195.061  1.00 54.63           O  
HETATM  330  O   HOH I2002     -38.571-104.059 192.743  1.00 43.71           O  
HETATM  331  O   HOH I2003     -18.753-106.895 192.088  1.00 32.11           O  
HETATM  332  O   HOH I2004     -26.958-108.149 186.724  1.00 42.64           O  
HETATM  333  O   HOH I2005     -37.008-101.474 193.666  1.00 46.15           O  
HETATM  334  O   HOH I2006     -38.073-101.322 197.366  1.00 38.31           O  
HETATM  335  O   HOH I2007     -16.973 -99.533 204.175  1.00 31.43           O  
HETATM  336  O   HOH I2008     -18.579-103.594 193.195  1.00 40.11           O  
HETATM  337  O   HOH I2009     -18.123-106.245 199.368  1.00 48.14           O  
HETATM  338  O   HOH I2010     -19.836-102.071 208.340  1.00 39.02           O  
HETATM  339  O   HOH I2011     -22.779-103.758 210.041  1.00 45.83           O  
HETATM  340  O   HOH I2012     -29.818-108.270 205.790  1.00 34.57           O  
HETATM  341  O   HOH I2013     -33.816-108.439 200.686  1.00 25.97           O  
HETATM  342  O   HOH I2014     -32.617-119.408 203.176  1.00 40.92           O  
HETATM  343  O   HOH I2015     -37.264-114.096 196.199  1.00 42.69           O  
HETATM  344  O   HOH I2016     -22.747 -96.690 201.988  1.00 38.47           O  
HETATM  345  O   HOH I2017     -36.689 -99.207 213.531  1.00 21.23           O  
HETATM  346  O   HOH I2018     -33.779-103.596 201.731  1.00 29.97           O  
HETATM  347  O   HOH I2019     -33.513 -94.874 201.979  1.00 24.09           O  
HETATM  348  O   HOH I2020     -40.100 -98.489 197.316  1.00 32.45           O  
HETATM  349  O   HOH I2021     -44.025 -96.355 188.795  1.00 40.49           O  
ENDMDL                                                                          
MASTER        0    0    0  124  120    0   73    625234   16    0  256          
END                                                                             
