HEADER    SIGNALING PROTEIN                       24-NOV-04   XXXX              
TITLE     STRUCTURE OF G-ALPHA-I1 BOUND TO A GDP-SELECTIVE PEPTIDE              
TITLE    2 PROVIDES INSIGHT INTO GUANINE NUCLEOTIDE EXCHANGE                    
COMPND    Guanine nucleotide-binding protein G(i), alpha-1 subunit,             
COMPND   2 KB752 peptide                                                        
KEYWDS    PROTEIN-PEPTIDE COMPLEX, SIGNALING PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.JOHNSTON, F.S.WILLARD, M.R.JEZYK, Z.FREDERICKS,                   
AUTHOR   2 E.T.BODOR, M.B.JONES, R.BLAESIUS, T.K.HARDEN, J.SONDEK,              
AUTHOR   3 V.J.WATTS, J.K.RAMER, D.P.SIDEROVSKI                                 
JRNL        AUTH   C.A.JOHNSTON, F.S.WILLARD, M.R.JEZYK, Z.FREDERICKS,          
JRNL        AUTH 2 E.T.BODOR, M.B.JONES, R.BLAESIUS, V.J.WATTS,                 
JRNL        AUTH 3 T.K.HARDEN, J.SONDEK, J.K.RAMER, D.P.SIDEROVSKI              
JRNL        TITL   STRUCTURE OF G-ALPHA-I1 BOUND TO A GDP-SELECTIVE             
JRNL        TITL 2 PEPTIDE PROVIDES INSIGHT INTO GUANINE NUCLEOTIDE             
JRNL        TITL 3 EXCHANGE                                                     
JRNL        REF    STRUCTURE                     V.   7  1069 2005              
JRNL        REFN   ASTM STRUE6  UK ISSN 0969-2126                               
JRNL        PMID   16004878                                                     
JRNL        DOI    10.1016/J.STR.2005.04.007                                    
SEQRES   1 A  329  ASP GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU          
SEQRES   2 A  329  LEU GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS          
SEQRES   3 A  329  GLN MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU          
SEQRES   4 A  329  GLU CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR          
SEQRES   5 A  329  ILE GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG          
SEQRES   6 A  329  LEU LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP          
SEQRES   7 A  329  ALA ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU          
SEQRES   8 A  329  GLY PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG          
SEQRES   9 A  329  LEU TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG          
SEQRES  10 A  329  SER ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR          
SEQRES  11 A  329  LEU ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE          
SEQRES  12 A  329  PRO THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR          
SEQRES  13 A  329  THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU          
SEQRES  14 A  329  HIS PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU          
SEQRES  15 A  329  ARG LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA          
SEQRES  16 A  329  ILE ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL          
SEQRES  17 A  329  LEU ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER          
SEQRES  18 A  329  MET LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE          
SEQRES  19 A  329  THR ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP          
SEQRES  20 A  329  LEU PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE          
SEQRES  21 A  329  CYS TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU          
SEQRES  22 A  329  ALA ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN          
SEQRES  23 A  329  LYS ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR          
SEQRES  24 A  329  CYS ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP          
SEQRES  25 A  329  ALA VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP          
SEQRES  26 A  329  CYS GLY LEU PHE                                              
SEQRES   1 B  329  ASP GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU          
SEQRES   2 B  329  LEU GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS          
SEQRES   3 B  329  GLN MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU          
SEQRES   4 B  329  GLU CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR          
SEQRES   5 B  329  ILE GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG          
SEQRES   6 B  329  LEU LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP          
SEQRES   7 B  329  ALA ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU          
SEQRES   8 B  329  GLY PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG          
SEQRES   9 B  329  LEU TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG          
SEQRES  10 B  329  SER ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR          
SEQRES  11 B  329  LEU ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE          
SEQRES  12 B  329  PRO THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR          
SEQRES  13 B  329  THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU          
SEQRES  14 B  329  HIS PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU          
SEQRES  15 B  329  ARG LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA          
SEQRES  16 B  329  ILE ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL          
SEQRES  17 B  329  LEU ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER          
SEQRES  18 B  329  MET LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE          
SEQRES  19 B  329  THR ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP          
SEQRES  20 B  329  LEU PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE          
SEQRES  21 B  329  CYS TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU          
SEQRES  22 B  329  ALA ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN          
SEQRES  23 B  329  LYS ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR          
SEQRES  24 B  329  CYS ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP          
SEQRES  25 B  329  ALA VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP          
SEQRES  26 B  329  CYS GLY LEU PHE                                              
SEQRES   1 C  329  ASP GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU          
SEQRES   2 C  329  LEU GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS          
SEQRES   3 C  329  GLN MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU          
SEQRES   4 C  329  GLU CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR          
SEQRES   5 C  329  ILE GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG          
SEQRES   6 C  329  LEU LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP          
SEQRES   7 C  329  ALA ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU          
SEQRES   8 C  329  GLY PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG          
SEQRES   9 C  329  LEU TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG          
SEQRES  10 C  329  SER ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR          
SEQRES  11 C  329  LEU ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE          
SEQRES  12 C  329  PRO THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR          
SEQRES  13 C  329  THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU          
SEQRES  14 C  329  HIS PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU          
SEQRES  15 C  329  ARG LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA          
SEQRES  16 C  329  ILE ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL          
SEQRES  17 C  329  LEU ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER          
SEQRES  18 C  329  MET LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE          
SEQRES  19 C  329  THR ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP          
SEQRES  20 C  329  LEU PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE          
SEQRES  21 C  329  CYS TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU          
SEQRES  22 C  329  ALA ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN          
SEQRES  23 C  329  LYS ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR          
SEQRES  24 C  329  CYS ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP          
SEQRES  25 C  329  ALA VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP          
SEQRES  26 C  329  CYS GLY LEU PHE                                              
SEQRES   1 D  329  ASP GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU          
SEQRES   2 D  329  LEU GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS          
SEQRES   3 D  329  GLN MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU          
SEQRES   4 D  329  GLU CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR          
SEQRES   5 D  329  ILE GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG          
SEQRES   6 D  329  LEU LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP          
SEQRES   7 D  329  ALA ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU          
SEQRES   8 D  329  GLY PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG          
SEQRES   9 D  329  LEU TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG          
SEQRES  10 D  329  SER ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR          
SEQRES  11 D  329  LEU ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE          
SEQRES  12 D  329  PRO THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR          
SEQRES  13 D  329  THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU          
SEQRES  14 D  329  HIS PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU          
SEQRES  15 D  329  ARG LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA          
SEQRES  16 D  329  ILE ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL          
SEQRES  17 D  329  LEU ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER          
SEQRES  18 D  329  MET LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE          
SEQRES  19 D  329  THR ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP          
SEQRES  20 D  329  LEU PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE          
SEQRES  21 D  329  CYS TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU          
SEQRES  22 D  329  ALA ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN          
SEQRES  23 D  329  LYS ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR          
SEQRES  24 D  329  CYS ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP          
SEQRES  25 D  329  ALA VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP          
SEQRES  26 D  329  CYS GLY LEU PHE                                              
SEQRES   1 E   16  SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR          
SEQRES   2 E   16  LYS SER ARG                                                  
SEQRES   1 F   16  SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR          
SEQRES   2 F   16  LYS SER ARG                                                  
SEQRES   1 G   16  SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR          
SEQRES   2 G   16  LYS SER ARG                                                  
SEQRES   1 H   16  SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR          
SEQRES   2 H   16  LYS SER ARG                                                  
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   9  GDP    4(C10 H15 N5 O11 P2)                                         
FORMUL  13  HOH   *136(H2 O)                                                    
HELIX    1   1 GLY A   45  GLU A   58  1                                  14    
HELIX    2   2 SER A   62  GLN A   68  1                                   7    
HELIX    3   3 TYR A   69  LEU A   91  1                                  23    
HELIX    4   4 ALA A   99  ALA A  111  1                                  13    
HELIX    5   5 THR A  120  ASP A  133  1                                  14    
HELIX    6   6 ASP A  133  ASN A  141  1                                   9    
HELIX    7   7 ARG A  142  TYR A  146  5                                   5    
HELIX    8   8 SER A  151  ASN A  157  1                                   7    
HELIX    9   9 ASP A  158  GLN A  164  1                                   7    
HELIX   10  10 THR A  170  THR A  177  1                                   8    
HELIX   11  11 ARG A  208  GLU A  216  1                                   9    
HELIX   12  12 SER A  228  LEU A  232  5                                   5    
HELIX   13  13 ASN A  241  ASN A  255  1                                  15    
HELIX   14  14 ASN A  256  THR A  260  5                                   5    
HELIX   15  15 LYS A  270  LYS A  279  1                                  10    
HELIX   16  16 PRO A  282  CYS A  286  5                                   5    
HELIX   17  17 THR A  295  ASP A  309  1                                  15    
HELIX   18  18 ASP A  328  LYS A  345  1                                  18    
HELIX   19  19 GLY B   45  GLU B   58  1                                  14    
HELIX   20  20 SER B   62  GLN B   68  1                                   7    
HELIX   21  21 TYR B   69  LEU B   91  1                                  23    
HELIX   22  22 ALA B   99  GLY B  112  1                                  14    
HELIX   23  23 THR B  120  ASP B  133  1                                  14    
HELIX   24  24 ASP B  133  ASN B  141  1                                   9    
HELIX   25  25 ARG B  142  TYR B  146  5                                   5    
HELIX   26  26 SER B  151  ASP B  158  1                                   8    
HELIX   27  27 ASP B  158  GLN B  164  1                                   7    
HELIX   28  28 THR B  170  THR B  177  1                                   8    
HELIX   29  29 GLU B  207  GLU B  216  1                                  10    
HELIX   30  30 SER B  228  TYR B  230  5                                   3    
HELIX   31  31 ASN B  241  ASN B  255  1                                  15    
HELIX   32  32 ASN B  256  THR B  260  5                                   5    
HELIX   33  33 LYS B  270  LYS B  279  1                                  10    
HELIX   34  34 PRO B  282  CYS B  286  5                                   5    
HELIX   35  35 THR B  295  ASP B  309  1                                  15    
HELIX   36  36 ASP B  328  ILE B  344  1                                  17    
HELIX   37  37 GLY C   45  GLU C   58  1                                  14    
HELIX   38  38 SER C   62  GLN C   68  1                                   7    
HELIX   39  39 TYR C   69  LEU C   91  1                                  23    
HELIX   40  40 ALA C   99  ALA C  111  1                                  13    
HELIX   41  41 THR C  120  ASP C  133  1                                  14    
HELIX   42  42 ASP C  133  ASN C  141  1                                   9    
HELIX   43  43 ARG C  142  TYR C  146  5                                   5    
HELIX   44  44 SER C  151  ASN C  157  1                                   7    
HELIX   45  45 ASP C  158  GLN C  164  1                                   7    
HELIX   46  46 THR C  170  THR C  177  1                                   8    
HELIX   47  47 ARG C  208  GLU C  216  1                                   9    
HELIX   48  48 SER C  228  TYR C  230  5                                   3    
HELIX   49  49 ASN C  241  ASN C  255  1                                  15    
HELIX   50  50 ASN C  256  THR C  260  5                                   5    
HELIX   51  51 LYS C  270  LYS C  279  1                                  10    
HELIX   52  52 PRO C  282  CYS C  286  5                                   5    
HELIX   53  53 THR C  295  ASP C  309  1                                  15    
HELIX   54  54 ASP C  328  ILE C  344  1                                  17    
HELIX   55  55 GLY D   45  GLU D   58  1                                  14    
HELIX   56  56 SER D   62  GLN D   68  1                                   7    
HELIX   57  57 TYR D   69  LEU D   91  1                                  23    
HELIX   58  58 ALA D   99  ALA D  111  1                                  13    
HELIX   59  59 THR D  120  ASP D  133  1                                  14    
HELIX   60  60 ASP D  133  ASN D  141  1                                   9    
HELIX   61  61 ARG D  142  TYR D  146  5                                   5    
HELIX   62  62 SER D  151  ASN D  157  1                                   7    
HELIX   63  63 ASP D  158  GLN D  164  1                                   7    
HELIX   64  64 THR D  170  THR D  177  1                                   8    
HELIX   65  65 GLU D  207  GLU D  216  1                                  10    
HELIX   66  66 SER D  228  LEU D  232  5                                   5    
HELIX   67  67 ASN D  241  ASN D  255  1                                  15    
HELIX   68  68 ASN D  256  THR D  260  5                                   5    
HELIX   69  69 LYS D  270  LYS D  279  1                                  10    
HELIX   70  70 PRO D  282  CYS D  286  5                                   5    
HELIX   71  71 THR D  295  ASP D  309  1                                  15    
HELIX   72  72 ASP D  328  ILE D  344  1                                  17    
HELIX   73  73 THR E    4  MET E   10  1                                   7    
HELIX   74  74 THR F    4  GLU F   11  1                                   8    
HELIX   75  75 THR G    4  GLU G   11  1                                   8    
HELIX   76  76 TRP H    5  MET H   10  1                                   6    
SHEET    1   A 6 VAL A 185  PHE A 191  0                                        
SHEET    2   A 6 LEU A 194  ASP A 200 -1  O  ASP A 200   N  VAL A 185           
SHEET    3   A 6 LYS A  35  GLY A  40  1  N  LEU A  36   O  LYS A 197           
SHEET    4   A 6 ALA A 220  ALA A 226  1  O  CYS A 224   N  LEU A  39           
SHEET    5   A 6 SER A 263  ASN A 269  1  O  ILE A 265   N  ILE A 221           
SHEET    6   A 6 ILE A 319  PHE A 323  1  O  HIS A 322   N  LEU A 268           
SHEET    1   B 2 SER A 206  GLU A 207  0                                        
SHEET    2   B 2 ARG E   2  VAL E   3 -1  O  VAL E   3   N  SER A 206           
SHEET    1   C 6 VAL B 185  PHE B 191  0                                        
SHEET    2   C 6 LEU B 194  ASP B 200 -1  O  ASP B 200   N  VAL B 185           
SHEET    3   C 6 LYS B  35  GLY B  40  1  N  LEU B  36   O  LYS B 197           
SHEET    4   C 6 ALA B 220  ALA B 226  1  O  CYS B 224   N  LEU B  39           
SHEET    5   C 6 SER B 263  ASN B 269  1  O  PHE B 267   N  PHE B 223           
SHEET    6   C 6 ILE B 319  PHE B 323  1  O  TYR B 320   N  LEU B 266           
SHEET    1   D 6 VAL C 185  PHE C 191  0                                        
SHEET    2   D 6 LEU C 194  ASP C 200 -1  O  ASP C 200   N  VAL C 185           
SHEET    3   D 6 LYS C  35  GLY C  40  1  N  LEU C  36   O  PHE C 199           
SHEET    4   D 6 ALA C 220  ALA C 226  1  O  CYS C 224   N  LEU C  39           
SHEET    5   D 6 SER C 263  ASN C 269  1  O  PHE C 267   N  PHE C 223           
SHEET    6   D 6 ILE C 319  PHE C 323  1  O  HIS C 322   N  LEU C 268           
SHEET    1   E 2 SER C 206  GLU C 207  0                                        
SHEET    2   E 2 ARG G   2  VAL G   3 -1  O  VAL G   3   N  SER C 206           
SHEET    1   F 6 VAL D 185  PHE D 191  0                                        
SHEET    2   F 6 LEU D 194  ASP D 200 -1  O  ASP D 200   N  VAL D 185           
SHEET    3   F 6 LYS D  35  GLY D  40  1  N  LEU D  38   O  PHE D 199           
SHEET    4   F 6 ALA D 220  ALA D 226  1  O  CYS D 224   N  LEU D  39           
SHEET    5   F 6 SER D 263  ASN D 269  1  O  PHE D 267   N  PHE D 223           
SHEET    6   F 6 ILE D 319  PHE D 323  1  O  HIS D 322   N  LEU D 268           
SHEET    1   G 2 ARG D 205  SER D 206  0                                        
SHEET    2   G 2 VAL H   3  THR H   4 -1  O  VAL H   3   N  SER D 206           
SITE     1 AC1 20 GLY A  42  GLU A  43  SER A  44  GLY A  45                    
SITE     2 AC1 20 LYS A  46  SER A  47  THR A  48  ASP A 150                    
SITE     3 AC1 20 LEU A 175  ARG A 176  ARG A 178  ASN A 269                    
SITE     4 AC1 20 LYS A 270  ASP A 272  LEU A 273  CYS A 325                    
SITE     5 AC1 20 ALA A 326  THR A 327  HOH A 358  HOH A 372                    
SITE     1 AC2 21 GLU B  43  SER B  44  GLY B  45  LYS B  46                    
SITE     2 AC2 21 SER B  47  THR B  48  ASP B 150  LEU B 175                    
SITE     3 AC2 21 ARG B 176  THR B 177  ARG B 178  ASN B 269                    
SITE     4 AC2 21 LYS B 270  ASP B 272  LEU B 273  CYS B 325                    
SITE     5 AC2 21 ALA B 326  THR B 327  HOH B 358  HOH B 365                    
SITE     6 AC2 21 HOH B 366                                                     
SITE     1 AC3 21 GLY C  42  GLU C  43  SER C  44  GLY C  45                    
SITE     2 AC3 21 LYS C  46  SER C  47  THR C  48  ASP C 150                    
SITE     3 AC3 21 LEU C 175  ARG C 176  THR C 177  ARG C 178                    
SITE     4 AC3 21 ASN C 269  LYS C 270  ASP C 272  LEU C 273                    
SITE     5 AC3 21 CYS C 325  ALA C 326  THR C 327  HOH C 362                    
SITE     6 AC3 21 HOH C 367                                                     
SITE     1 AC4 21 GLY D  42  GLU D  43  SER D  44  GLY D  45                    
SITE     2 AC4 21 LYS D  46  SER D  47  THR D  48  ASP D 150                    
SITE     3 AC4 21 LEU D 175  ARG D 176  THR D 177  ARG D 178                    
SITE     4 AC4 21 ASN D 269  LYS D 270  ASP D 272  LEU D 273                    
SITE     5 AC4 21 CYS D 325  ALA D 326  THR D 327  HOH D 372                    
SITE     6 AC4 21 HOH D 374                                                     
CRYST1   72.943  112.785  109.490  90.00  93.75  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013709  0.000000  0.000899        0.00000                         
SCALE2      0.000000  0.008866  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009153        0.00000                         
MODEL        1                                                                  
ATOM      1  N   SER G   1      20.706  50.675  38.901  1.00 92.82           N  
ATOM      2  CA  SER G   1      20.552  52.077  38.421  1.00 89.78           C  
ATOM      3  C   SER G   1      21.783  52.887  38.805  1.00 89.55           C  
ATOM      4  O   SER G   1      22.441  53.475  37.947  1.00 90.05           O  
ATOM      5  CB  SER G   1      19.302  52.709  39.037  1.00 94.39           C  
ATOM      6  OG  SER G   1      18.143  51.948  38.734  1.00 91.44           O  
ATOM      7  N   ARG G   2      22.085  52.908  40.100  1.00 62.97           N  
ATOM      8  CA  ARG G   2      23.239  53.635  40.620  1.00 60.15           C  
ATOM      9  C   ARG G   2      24.328  52.661  41.053  1.00 58.53           C  
ATOM     10  O   ARG G   2      24.108  51.791  41.886  1.00 57.04           O  
ATOM     11  CB  ARG G   2      22.808  54.528  41.790  1.00 59.31           C  
ATOM     12  CG  ARG G   2      22.059  55.777  41.334  1.00 61.04           C  
ATOM     13  CD  ARG G   2      21.263  56.456  42.440  1.00 62.43           C  
ATOM     14  NE  ARG G   2      22.072  56.780  43.611  1.00 62.46           N  
ATOM     15  CZ  ARG G   2      22.032  56.095  44.750  1.00 62.50           C  
ATOM     16  NH1 ARG G   2      21.222  55.051  44.864  1.00 62.26           N  
ATOM     17  NH2 ARG G   2      22.795  56.451  45.774  1.00 61.19           N  
ATOM     18  N   VAL G   3      25.509  52.807  40.473  1.00 42.10           N  
ATOM     19  CA  VAL G   3      26.606  51.916  40.793  1.00 41.58           C  
ATOM     20  C   VAL G   3      27.869  52.708  41.078  1.00 40.85           C  
ATOM     21  O   VAL G   3      27.936  53.899  40.790  1.00 41.68           O  
ATOM     22  CB  VAL G   3      26.865  50.954  39.622  1.00 55.53           C  
ATOM     23  CG1 VAL G   3      25.570  50.295  39.213  1.00 58.50           C  
ATOM     24  CG2 VAL G   3      27.451  51.706  38.445  1.00 56.32           C  
ATOM     25  N   THR G   4      28.867  52.047  41.654  1.00 57.58           N  
ATOM     26  CA  THR G   4      30.134  52.701  41.961  1.00 54.72           C  
ATOM     27  C   THR G   4      30.956  52.735  40.683  1.00 52.76           C  
ATOM     28  O   THR G   4      30.714  51.945  39.769  1.00 51.76           O  
ATOM     29  CB  THR G   4      30.929  51.932  43.036  1.00 48.43           C  
ATOM     30  OG1 THR G   4      31.338  50.661  42.515  1.00 48.26           O  
ATOM     31  CG2 THR G   4      30.076  51.716  44.271  1.00 49.19           C  
ATOM     32  N   TRP G   5      31.931  53.637  40.618  1.00 47.57           N  
ATOM     33  CA  TRP G   5      32.749  53.735  39.420  1.00 45.00           C  
ATOM     34  C   TRP G   5      33.486  52.435  39.115  1.00 43.28           C  
ATOM     35  O   TRP G   5      33.834  52.167  37.966  1.00 42.83           O  
ATOM     36  CB  TRP G   5      33.741  54.909  39.515  1.00 46.69           C  
ATOM     37  CG  TRP G   5      34.781  54.825  40.598  1.00 44.51           C  
ATOM     38  CD1 TRP G   5      34.770  55.479  41.794  1.00 44.84           C  
ATOM     39  CD2 TRP G   5      36.011  54.091  40.556  1.00 42.99           C  
ATOM     40  NE1 TRP G   5      35.916  55.204  42.496  1.00 43.66           N  
ATOM     41  CE2 TRP G   5      36.696  54.354  41.760  1.00 42.37           C  
ATOM     42  CE3 TRP G   5      36.601  53.238  39.616  1.00 43.07           C  
ATOM     43  CZ2 TRP G   5      37.941  53.796  42.051  1.00 42.41           C  
ATOM     44  CZ3 TRP G   5      37.838  52.683  39.904  1.00 42.74           C  
ATOM     45  CH2 TRP G   5      38.496  52.966  41.115  1.00 42.90           C  
ATOM     46  N   TYR G   6      33.719  51.623  40.140  1.00 41.05           N  
ATOM     47  CA  TYR G   6      34.400  50.353  39.937  1.00 38.69           C  
ATOM     48  C   TYR G   6      33.490  49.357  39.223  1.00 37.45           C  
ATOM     49  O   TYR G   6      33.913  48.675  38.293  1.00 37.87           O  
ATOM     50  CB  TYR G   6      34.843  49.743  41.264  1.00 34.06           C  
ATOM     51  CG  TYR G   6      35.562  48.436  41.053  1.00 31.84           C  
ATOM     52  CD1 TYR G   6      36.861  48.413  40.552  1.00 30.96           C  
ATOM     53  CD2 TYR G   6      34.915  47.219  41.267  1.00 30.70           C  
ATOM     54  CE1 TYR G   6      37.497  47.216  40.263  1.00 31.66           C  
ATOM     55  CE2 TYR G   6      35.543  46.014  40.979  1.00 30.09           C  
ATOM     56  CZ  TYR G   6      36.831  46.022  40.476  1.00 31.17           C  
ATOM     57  OH  TYR G   6      37.456  44.840  40.162  1.00 31.15           O  
ATOM     58  N   ASP G   7      32.245  49.261  39.675  1.00 34.77           N  
ATOM     59  CA  ASP G   7      31.300  48.350  39.054  1.00 35.39           C  
ATOM     60  C   ASP G   7      31.013  48.837  37.644  1.00 35.23           C  
ATOM     61  O   ASP G   7      30.787  48.041  36.737  1.00 33.70           O  
ATOM     62  CB  ASP G   7      30.002  48.273  39.858  1.00 51.34           C  
ATOM     63  CG  ASP G   7      30.185  47.573  41.189  1.00 50.60           C  
ATOM     64  OD1 ASP G   7      31.088  46.716  41.293  1.00 49.31           O  
ATOM     65  OD2 ASP G   7      29.418  47.870  42.128  1.00 51.17           O  
ATOM     66  N   PHE G   8      31.039  50.151  37.467  1.00 43.43           N  
ATOM     67  CA  PHE G   8      30.801  50.747  36.163  1.00 45.21           C  
ATOM     68  C   PHE G   8      31.915  50.416  35.177  1.00 45.98           C  
ATOM     69  O   PHE G   8      31.653  50.188  33.995  1.00 46.73           O  
ATOM     70  CB  PHE G   8      30.689  52.262  36.277  1.00 46.29           C  
ATOM     71  CG  PHE G   8      30.728  52.958  34.959  1.00 47.42           C  
ATOM     72  CD1 PHE G   8      29.625  52.936  34.115  1.00 46.91           C  
ATOM     73  CD2 PHE G   8      31.886  53.601  34.536  1.00 48.85           C  
ATOM     74  CE1 PHE G   8      29.670  53.543  32.870  1.00 47.48           C  
ATOM     75  CE2 PHE G   8      31.942  54.212  33.288  1.00 50.31           C  
ATOM     76  CZ  PHE G   8      30.830  54.182  32.453  1.00 48.90           C  
ATOM     77  N   LEU G   9      33.157  50.407  35.656  1.00 43.26           N  
ATOM     78  CA  LEU G   9      34.297  50.102  34.801  1.00 44.06           C  
ATOM     79  C   LEU G   9      34.366  48.621  34.483  1.00 45.98           C  
ATOM     80  O   LEU G   9      34.849  48.230  33.424  1.00 45.40           O  
ATOM     81  CB  LEU G   9      35.609  50.528  35.462  1.00 37.08           C  
ATOM     82  CG  LEU G   9      35.903  52.019  35.613  1.00 37.58           C  
ATOM     83  CD1 LEU G   9      37.295  52.203  36.190  1.00 36.31           C  
ATOM     84  CD2 LEU G   9      35.803  52.704  34.272  1.00 37.46           C  
ATOM     85  N   MET G  10      33.882  47.793  35.397  1.00 46.14           N  
ATOM     86  CA  MET G  10      33.914  46.354  35.181  1.00 48.74           C  
ATOM     87  C   MET G  10      32.721  45.831  34.383  1.00 51.12           C  
ATOM     88  O   MET G  10      32.704  44.668  33.983  1.00 50.36           O  
ATOM     89  CB  MET G  10      34.008  45.624  36.523  1.00 51.35           C  
ATOM     90  CG  MET G  10      35.286  45.925  37.284  1.00 49.48           C  
ATOM     91  SD  MET G  10      36.747  45.588  36.290  1.00 43.04           S  
ATOM     92  CE  MET G  10      36.996  43.874  36.641  1.00 44.90           C  
ATOM     93  N   GLU G  11      31.732  46.692  34.150  1.00 59.91           N  
ATOM     94  CA  GLU G  11      30.536  46.324  33.390  1.00 63.75           C  
ATOM     95  C   GLU G  11      30.892  45.846  31.981  1.00 64.75           C  
ATOM     96  O   GLU G  11      31.446  46.604  31.184  1.00 63.55           O  
ATOM     97  CB  GLU G  11      29.582  47.520  33.283  1.00 82.07           C  
ATOM     98  CG  GLU G  11      28.349  47.456  34.180  1.00 83.02           C  
ATOM     99  CD  GLU G  11      27.330  48.546  33.853  1.00 83.88           C  
ATOM    100  OE1 GLU G  11      27.634  49.744  34.042  1.00 82.18           O  
ATOM    101  OE2 GLU G  11      26.218  48.203  33.400  1.00 84.63           O  
ATOM    102  N   ASP G  12      30.567  44.593  31.672  1.00 85.38           N  
ATOM    103  CA  ASP G  12      30.856  44.050  30.350  1.00 87.37           C  
ATOM    104  C   ASP G  12      29.768  44.460  29.352  1.00 86.55           C  
ATOM    105  O   ASP G  12      28.572  44.236  29.576  1.00 84.73           O  
ATOM    106  CB  ASP G  12      30.958  42.516  30.393  1.00174.27           C  
ATOM    107  CG  ASP G  12      32.181  42.016  31.166  1.00174.65           C  
ATOM    108  OD1 ASP G  12      33.253  42.665  31.094  1.00174.65           O  
ATOM    109  OD2 ASP G  12      32.071  40.954  31.830  1.00175.14           O  
TER     110      ASP G  12                                                      
HETATM  111  O   HOH G  60      34.328  52.685  43.385  1.00 43.67           O  
HETATM  112  O   HOH G  63      23.307  51.265  44.129  1.00 43.24           O  
ENDMDL                                                                          
MASTER        0    0    0   76   30    0   23    610424    8    0  112          
END                                                                             
