HEADER    IMMUNE SYSTEM/INHIBITOR                 04-MAR-10   XXXX              
TITLE     CRYSTAL STRUCTURE OF HUMAN FCRN WITH A MONOMERIC PEPTIDE INHIBITOR    
KEYWDS    IMMUNOGLOBULIN BINDING PROTEIN, CELL MEMBRANE, DISULFIDE BOND,        
KEYWDS   2 GLYCOPROTEIN, IGG-BINDING PROTEIN, IMMUNOGLOBULIN DOMAIN, MEMBRANE,  
KEYWDS   3 RECEPTOR, TRANSMEMBRANE, AMYLOID, AMYLOIDOSIS, DISEASE MUTATION,     
KEYWDS   4 GLYCATION, IMMUNE RESPONSE, MHC I, PYRROLIDONE CARBOXYLIC ACID,      
KEYWDS   5 SECRETED, IMMUNE SYSTEM-INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.R.MEZO, V.SRIDHAR, J.BADGER, P.SAKORAFAS, V.NIENABER                
JRNL        AUTH   A.R.MEZO, V.SRIDHAR, J.BADGER, P.SAKORAFAS, V.NIENABER       
JRNL        TITL   X-RAY CRYSTAL STRUCTURES OF MONOMERIC AND DIMERIC PEPTIDE    
JRNL        TITL 2 INHIBITORS IN COMPLEX WITH THE HUMAN NEONATAL FC RECEPTOR,   
JRNL        TITL 3 FCRN.                                                        
JRNL        REF    J.BIOL.CHEM.                  V. 285 27694 2010              
JRNL        REFN   ASTM JBCHA3  US ISSN 0021-9258                               
JRNL        PMID   20592032                                                     
JRNL        DOI    10.1074/JBC.M110.120667                                      
SEQRES   1 A  267  ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA          
SEQRES   2 A  267  VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL          
SEQRES   3 A  267  SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN          
SEQRES   4 A  267  SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL          
SEQRES   5 A  267  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 A  267  THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA          
SEQRES   7 A  267  PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN          
SEQRES   8 A  267  GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER          
SEQRES   9 A  267  VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE          
SEQRES  10 A  267  MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP          
SEQRES  11 A  267  TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN          
SEQRES  12 A  267  GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU          
SEQRES  13 A  267  PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG          
SEQRES  14 A  267  GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET          
SEQRES  15 A  267  ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL          
SEQRES  16 A  267  LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU          
SEQRES  17 A  267  GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR          
SEQRES  18 A  267  GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE          
SEQRES  19 A  267  HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU          
SEQRES  20 A  267  HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA          
SEQRES  21 A  267  GLN PRO LEU ARG VAL GLU LEU                                  
SEQRES   1 B   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C  267  ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA          
SEQRES   2 C  267  VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL          
SEQRES   3 C  267  SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN          
SEQRES   4 C  267  SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL          
SEQRES   5 C  267  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 C  267  THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA          
SEQRES   7 C  267  PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN          
SEQRES   8 C  267  GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER          
SEQRES   9 C  267  VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE          
SEQRES  10 C  267  MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP          
SEQRES  11 C  267  TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN          
SEQRES  12 C  267  GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU          
SEQRES  13 C  267  PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG          
SEQRES  14 C  267  GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET          
SEQRES  15 C  267  ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL          
SEQRES  16 C  267  LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU          
SEQRES  17 C  267  GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR          
SEQRES  18 C  267  GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE          
SEQRES  19 C  267  HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU          
SEQRES  20 C  267  HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA          
SEQRES  21 C  267  GLN PRO LEU ARG VAL GLU LEU                                  
SEQRES   1 D   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 D   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 D   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 D   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 D   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 D   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 D   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 D   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 E  267  ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA          
SEQRES   2 E  267  VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL          
SEQRES   3 E  267  SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN          
SEQRES   4 E  267  SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL          
SEQRES   5 E  267  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 E  267  THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA          
SEQRES   7 E  267  PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN          
SEQRES   8 E  267  GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER          
SEQRES   9 E  267  VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE          
SEQRES  10 E  267  MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP          
SEQRES  11 E  267  TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN          
SEQRES  12 E  267  GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU          
SEQRES  13 E  267  PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG          
SEQRES  14 E  267  GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET          
SEQRES  15 E  267  ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL          
SEQRES  16 E  267  LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU          
SEQRES  17 E  267  GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR          
SEQRES  18 E  267  GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE          
SEQRES  19 E  267  HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU          
SEQRES  20 E  267  HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA          
SEQRES  21 E  267  GLN PRO LEU ARG VAL GLU LEU                                  
SEQRES   1 F   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 F   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 F   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 F   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 F   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 F   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 F   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 F   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 G  267  ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA          
SEQRES   2 G  267  VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL          
SEQRES   3 G  267  SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN          
SEQRES   4 G  267  SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL          
SEQRES   5 G  267  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 G  267  THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA          
SEQRES   7 G  267  PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN          
SEQRES   8 G  267  GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER          
SEQRES   9 G  267  VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE          
SEQRES  10 G  267  MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP          
SEQRES  11 G  267  TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN          
SEQRES  12 G  267  GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU          
SEQRES  13 G  267  PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG          
SEQRES  14 G  267  GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET          
SEQRES  15 G  267  ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL          
SEQRES  16 G  267  LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU          
SEQRES  17 G  267  GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR          
SEQRES  18 G  267  GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE          
SEQRES  19 G  267  HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU          
SEQRES  20 G  267  HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA          
SEQRES  21 G  267  GLN PRO LEU ARG VAL GLU LEU                                  
SEQRES   1 H   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 H   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 H   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 H   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 H   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 H   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 H   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 H   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 I   15  ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO          
SEQRES   2 I   15  CYS NH2                                                      
SEQRES   1 J   15  ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO          
SEQRES   2 J   15  CYS NH2                                                      
SEQRES   1 K   15  ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO          
SEQRES   2 K   15  CYS NH2                                                      
SEQRES   1 L   15  ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO          
SEQRES   2 L   15  CYS NH2                                                      
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     LE1 3-SULFANYL-L-VALINE                                              
HETNAM     SAR SARCOSINE                                                        
HETNAM     MLE N-METHYLLEUCINE                                                  
HETNAM     NH2 AMINO GROUP                                                      
HETSYN     LE1 L-LE1ICILLAMINE                                                  
FORMUL   9  ACE    4(C2 H4 O)                                                   
FORMUL   9  LE1    4(C5 H11 N O2 S)                                             
FORMUL   9  SAR    4(C3 H7 N O2)                                                
FORMUL   9  MLE    4(C7 H15 N O2)                                               
FORMUL   9  NH2    4(H2 N)                                                      
FORMUL  13  HOH   *183(H2 O)                                                    
HELIX    1   1 GLY A   49  GLU A   54  5                                   6    
HELIX    2   2 TRP A   59  PHE A   79  1                                  21    
HELIX    3   3 LYS A   80  LEU A   82  5                                   3    
HELIX    4   4 TRP A  131  GLN A  144  1                                  14    
HELIX    5   5 LYS A  146  PHE A  157  1                                  12    
HELIX    6   6 PHE A  157  GLY A  170  1                                  14    
HELIX    7   7 GLY A  170  TRP A  176  1                                   7    
HELIX    8   8 ASP A  246  HIS A  248  5                                   3    
HELIX    9   9 GLY C   49  GLU C   54  5                                   6    
HELIX   10  10 TRP C   59  PHE C   79  1                                  21    
HELIX   11  11 LYS C   80  LEU C   82  5                                   3    
HELIX   12  12 TRP C  131  GLN C  143  1                                  13    
HELIX   13  13 LYS C  146  PHE C  157  1                                  12    
HELIX   14  14 PHE C  157  GLY C  170  1                                  14    
HELIX   15  15 GLY C  170  GLU C  175  1                                   6    
HELIX   16  16 ASP C  246  HIS C  248  5                                   3    
HELIX   17  17 GLY E   49  GLU E   54  5                                   6    
HELIX   18  18 TRP E   59  PHE E   79  1                                  21    
HELIX   19  19 LYS E   80  LEU E   82  5                                   3    
HELIX   20  20 TRP E  131  GLN E  144  1                                  14    
HELIX   21  21 LYS E  146  PHE E  157  1                                  12    
HELIX   22  22 PHE E  157  GLY E  170  1                                  14    
HELIX   23  23 GLY E  170  GLU E  175  1                                   6    
HELIX   24  24 GLY G   49  GLU G   54  5                                   6    
HELIX   25  25 TRP G   59  PHE G   79  1                                  21    
HELIX   26  26 LYS G   80  LEU G   82  5                                   3    
HELIX   27  27 TRP G  131  GLN G  144  1                                  14    
HELIX   28  28 LYS G  146  PHE G  157  1                                  12    
HELIX   29  29 PHE G  157  GLY G  170  1                                  14    
HELIX   30  30 GLY G  170  GLU G  175  1                                   6    
SHEET    1   A 8 GLU A  46  PRO A  47  0                                        
SHEET    2   A 8 GLN A  33  ASN A  39 -1  N  SER A  37   O  GLU A  46           
SHEET    3   A 8 PHE A  24  LEU A  30 -1  N  LEU A  30   O  GLN A  33           
SHEET    4   A 8 LEU A   7  VAL A  14 -1  N  HIS A  10   O  SER A  27           
SHEET    5   A 8 THR A  89  LEU A  98 -1  O  LEU A  94   N  TYR A   9           
SHEET    6   A 8 SER A 104  LEU A 112 -1  O  LYS A 109   N  LEU A  93           
SHEET    7   A 8 GLU A 115  ASP A 121 -1  O  GLU A 115   N  LEU A 112           
SHEET    8   A 8 THR A 126  GLY A 128 -1  O  THR A 126   N  ASP A 121           
SHEET    1   B 4 SER A 181  PRO A 188  0                                        
SHEET    2   B 4 PHE A 193  PHE A 203 -1  O  VAL A 195   N  ARG A 187           
SHEET    3   B 4 PHE A 234  LYS A 243 -1  O  VAL A 242   N  SER A 194           
SHEET    4   B 4 ASP A 225  PRO A 228 -1  N  GLY A 227   O  HIS A 235           
SHEET    1   C 4 LEU A 217  GLY A 220  0                                        
SHEET    2   C 4 GLN A 209  ARG A 214 -1  N  ARG A 214   O  LEU A 217           
SHEET    3   C 4 TYR A 250  GLN A 255 -1  O  ILE A 253   N  ARG A 211           
SHEET    4   C 4 LEU A 263  VAL A 265 -1  O  VAL A 265   N  CYS A 252           
SHEET    1   D 4 LYS B   6  SER B  11  0                                        
SHEET    2   D 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   D 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4   D 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1   E 4 LYS B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4   E 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   F 4 GLU B  44  ARG B  45  0                                        
SHEET    2   F 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   F 4 TYR B  78  ASN B  83 -1  O  ARG B  81   N  ASP B  38           
SHEET    4   F 4 LYS B  91  LYS B  94 -1  O  VAL B  93   N  CYS B  80           
SHEET    1   G 8 GLU C  46  PRO C  47  0                                        
SHEET    2   G 8 GLN C  33  ASN C  39 -1  N  SER C  37   O  GLU C  46           
SHEET    3   G 8 PHE C  24  LEU C  30 -1  N  VAL C  26   O  TYR C  38           
SHEET    4   G 8 SER C   6  VAL C  14 -1  N  HIS C  10   O  SER C  27           
SHEET    5   G 8 THR C  89  LEU C  98 -1  O  LEU C  94   N  TYR C   9           
SHEET    6   G 8 SER C 104  LEU C 112 -1  O  LYS C 109   N  LEU C  93           
SHEET    7   G 8 GLU C 115  ASP C 121 -1  O  MET C 118   N  PHE C 110           
SHEET    8   G 8 THR C 126  GLY C 128 -1  O  THR C 126   N  ASP C 121           
SHEET    1   H 4 SER C 181  PRO C 188  0                                        
SHEET    2   H 4 PHE C 193  PHE C 203 -1  O  VAL C 195   N  ARG C 187           
SHEET    3   H 4 PHE C 234  LYS C 243 -1  O  ALA C 236   N  ALA C 200           
SHEET    4   H 4 GLN C 223  PRO C 228 -1  N  GLY C 227   O  HIS C 235           
SHEET    1   I 4 LEU C 217  ALA C 218  0                                        
SHEET    2   I 4 GLN C 209  ARG C 214 -1  N  ARG C 214   O  LEU C 217           
SHEET    3   I 4 TYR C 250  GLN C 255 -1  O  ILE C 253   N  ARG C 211           
SHEET    4   I 4 LEU C 263  VAL C 265 -1  O  VAL C 265   N  CYS C 252           
SHEET    1   J 4 LYS D   6  SER D  11  0                                        
SHEET    2   J 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3   J 4 PHE D  62  PHE D  70 -1  O  LEU D  64   N  VAL D  27           
SHEET    4   J 4 GLU D  50  HIS D  51 -1  N  GLU D  50   O  TYR D  67           
SHEET    1   K 4 LYS D   6  SER D  11  0                                        
SHEET    2   K 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3   K 4 PHE D  62  PHE D  70 -1  O  LEU D  64   N  VAL D  27           
SHEET    4   K 4 SER D  55  PHE D  56 -1  N  SER D  55   O  TYR D  63           
SHEET    1   L 4 GLU D  44  ARG D  45  0                                        
SHEET    2   L 4 GLU D  36  LYS D  41 -1  N  LYS D  41   O  GLU D  44           
SHEET    3   L 4 TYR D  78  ASN D  83 -1  O  ASN D  83   N  GLU D  36           
SHEET    4   L 4 LYS D  91  LYS D  94 -1  O  LYS D  91   N  VAL D  82           
SHEET    1   M 8 GLU E  46  PRO E  47  0                                        
SHEET    2   M 8 GLN E  33  ASN E  39 -1  N  SER E  37   O  GLU E  46           
SHEET    3   M 8 PHE E  24  LEU E  30 -1  N  VAL E  26   O  TYR E  38           
SHEET    4   M 8 SER E   6  VAL E  14 -1  N  HIS E  10   O  SER E  27           
SHEET    5   M 8 THR E  89  LEU E  98 -1  O  LEU E  94   N  TYR E   9           
SHEET    6   M 8 SER E 104  LEU E 112 -1  O  LYS E 109   N  LEU E  93           
SHEET    7   M 8 GLU E 115  ASP E 121 -1  O  MET E 118   N  PHE E 110           
SHEET    8   M 8 THR E 126  GLY E 128 -1  O  THR E 126   N  ASP E 121           
SHEET    1   N 4 SER E 181  PRO E 188  0                                        
SHEET    2   N 4 PHE E 193  PHE E 203 -1  O  VAL E 195   N  ARG E 187           
SHEET    3   N 4 PHE E 234  LYS E 243 -1  O  ALA E 236   N  ALA E 200           
SHEET    4   N 4 GLN E 223  PRO E 228 -1  N  GLN E 223   O  SER E 239           
SHEET    1   O 4 LEU E 217  ALA E 218  0                                        
SHEET    2   O 4 GLN E 209  ARG E 214 -1  N  ARG E 214   O  LEU E 217           
SHEET    3   O 4 TYR E 250  GLN E 255 -1  O  CYS E 251   N  LEU E 213           
SHEET    4   O 4 LEU E 263  GLU E 266 -1  O  VAL E 265   N  CYS E 252           
SHEET    1   P 4 LYS F   6  SER F  11  0                                        
SHEET    2   P 4 ASN F  21  PHE F  30 -1  O  SER F  28   N  LYS F   6           
SHEET    3   P 4 PHE F  62  PHE F  70 -1  O  TYR F  66   N  CYS F  25           
SHEET    4   P 4 GLU F  50  HIS F  51 -1  N  GLU F  50   O  TYR F  67           
SHEET    1   Q 4 LYS F   6  SER F  11  0                                        
SHEET    2   Q 4 ASN F  21  PHE F  30 -1  O  SER F  28   N  LYS F   6           
SHEET    3   Q 4 PHE F  62  PHE F  70 -1  O  TYR F  66   N  CYS F  25           
SHEET    4   Q 4 SER F  55  PHE F  56 -1  N  SER F  55   O  TYR F  63           
SHEET    1   R 4 GLU F  44  ARG F  45  0                                        
SHEET    2   R 4 GLU F  36  LYS F  41 -1  N  LYS F  41   O  GLU F  44           
SHEET    3   R 4 TYR F  78  HIS F  84 -1  O  ARG F  81   N  ASP F  38           
SHEET    4   R 4 LEU F  87  LYS F  94 -1  O  VAL F  93   N  CYS F  80           
SHEET    1   S 8 GLU G  46  PRO G  47  0                                        
SHEET    2   S 8 GLN G  33  ASN G  39 -1  N  SER G  37   O  GLU G  46           
SHEET    3   S 8 PHE G  24  LEU G  30 -1  N  LEU G  30   O  GLN G  33           
SHEET    4   S 8 SER G   6  VAL G  14 -1  N  HIS G  10   O  SER G  27           
SHEET    5   S 8 THR G  89  GLU G  97 -1  O  LEU G  94   N  TYR G   9           
SHEET    6   S 8 THR G 107  LEU G 112 -1  O  LYS G 109   N  LEU G  93           
SHEET    7   S 8 GLU G 115  ASP G 121 -1  O  PHE G 117   N  PHE G 110           
SHEET    8   S 8 THR G 126  GLY G 128 -1  O  THR G 126   N  ASP G 121           
SHEET    1   T 4 SER G 181  PRO G 188  0                                        
SHEET    2   T 4 SER G 194  PHE G 203 -1  O  VAL G 195   N  ARG G 187           
SHEET    3   T 4 PHE G 234  VAL G 242 -1  O  VAL G 242   N  SER G 194           
SHEET    4   T 4 PHE G 226  PRO G 228 -1  N  GLY G 227   O  HIS G 235           
SHEET    1   U 4 LEU G 217  GLY G 220  0                                        
SHEET    2   U 4 GLN G 209  ARG G 214 -1  N  ARG G 214   O  LEU G 217           
SHEET    3   U 4 TYR G 250  GLN G 255 -1  O  ILE G 253   N  ARG G 211           
SHEET    4   U 4 LEU G 263  GLU G 266 -1  O  VAL G 265   N  CYS G 252           
SHEET    1   V 4 LYS H   6  SER H  11  0                                        
SHEET    2   V 4 ASN H  21  PHE H  30 -1  O  SER H  28   N  LYS H   6           
SHEET    3   V 4 PHE H  62  PHE H  70 -1  O  TYR H  66   N  CYS H  25           
SHEET    4   V 4 GLU H  50  HIS H  51 -1  N  GLU H  50   O  TYR H  67           
SHEET    1   W 4 LYS H   6  SER H  11  0                                        
SHEET    2   W 4 ASN H  21  PHE H  30 -1  O  SER H  28   N  LYS H   6           
SHEET    3   W 4 PHE H  62  PHE H  70 -1  O  TYR H  66   N  CYS H  25           
SHEET    4   W 4 SER H  55  PHE H  56 -1  N  SER H  55   O  TYR H  63           
SHEET    1   X 4 GLU H  44  ARG H  45  0                                        
SHEET    2   X 4 GLU H  36  LYS H  41 -1  N  LYS H  41   O  GLU H  44           
SHEET    3   X 4 TYR H  78  ASN H  83 -1  O  ARG H  81   N  ASP H  38           
SHEET    4   X 4 LYS H  91  LYS H  94 -1  O  LYS H  91   N  VAL H  82           
SHEET    1   Y 2 PHE I   2  THR I   4  0                                        
SHEET    2   Y 2 MLE I  10  PRO I  12 -1  O  TYR I  11   N  LE1 I   3           
SHEET    1   Z 2 PHE J   2  THR J   4  0                                        
SHEET    2   Z 2 MLE J  10  PRO J  12 -1  O  TYR J  11   N  LE1 J   3           
SHEET    1  AA 2 PHE K   2  THR K   4  0                                        
SHEET    2  AA 2 MLE K  10  PRO K  12 -1  O  TYR K  11   N  LE1 K   3           
SHEET    1  AB 2 PHE L   2  THR L   4  0                                        
SHEET    2  AB 2 MLE L  10  PRO L  12 -1  O  TYR L  11   N  LE1 L   3           
SSBOND   1 CYS A   96    CYS A  159                          1555   1555  2.05  
SSBOND   2 CYS A  198    CYS A  252                          1555   1555  2.02  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C   96    CYS C  159                          1555   1555  2.04  
SSBOND   5 CYS C  198    CYS C  252                          1555   1555  2.04  
SSBOND   6 CYS D   25    CYS D   80                          1555   1555  2.02  
SSBOND   7 CYS E   96    CYS E  159                          1555   1555  2.04  
SSBOND   8 CYS E  198    CYS E  252                          1555   1555  2.03  
SSBOND   9 CYS F   25    CYS F   80                          1555   1555  2.04  
SSBOND  10 CYS G   96    CYS G  159                          1555   1555  2.04  
SSBOND  11 CYS G  198    CYS G  252                          1555   1555  2.03  
SSBOND  12 CYS H   25    CYS H   80                          1555   1555  2.03  
SSBOND  13 LE1 I    3    CYS I   13                          1555   1555  2.04  
SSBOND  14 LE1 J    3    CYS J   13                          1555   1555  2.04  
SSBOND  15 LE1 K    3    CYS K   13                          1555   1555  2.03  
SSBOND  16 LE1 L    3    CYS L   13                          1555   1555  2.04  
LINK         C   ACE I   0                 N   ARG I   1     1555   1555  1.33  
LINK         C   PHE I   2                 N   LE1 I   3     1555   1555  1.33  
LINK         C   LE1 I   3                 N   THR I   4     1555   1555  1.33  
LINK         C   GLY I   8                 N   SAR I   9     1555   1555  1.34  
LINK         C   SAR I   9                 N   MLE I  10     1555   1555  1.34  
LINK         C   MLE I  10                 N   TYR I  11     1555   1555  1.33  
LINK         C   CYS I  13                 N   NH2 I  14     1555   1555  1.33  
LINK         C   ACE J   0                 N   ARG J   1     1555   1555  1.33  
LINK         C   PHE J   2                 N   LE1 J   3     1555   1555  1.33  
LINK         C   LE1 J   3                 N   THR J   4     1555   1555  1.33  
LINK         C   GLY J   8                 N   SAR J   9     1555   1555  1.34  
LINK         C   SAR J   9                 N   MLE J  10     1555   1555  1.33  
LINK         C   MLE J  10                 N   TYR J  11     1555   1555  1.33  
LINK         C   CYS J  13                 N   NH2 J  14     1555   1555  1.32  
LINK         C   ACE K   0                 N   ARG K   1     1555   1555  1.33  
LINK         C   PHE K   2                 N   LE1 K   3     1555   1555  1.33  
LINK         C   LE1 K   3                 N   THR K   4     1555   1555  1.33  
LINK         C   GLY K   8                 N   SAR K   9     1555   1555  1.34  
LINK         C   SAR K   9                 N   MLE K  10     1555   1555  1.34  
LINK         C   MLE K  10                 N   TYR K  11     1555   1555  1.33  
LINK         C   CYS K  13                 N   NH2 K  14     1555   1555  1.36  
LINK         C   ACE L   0                 N   ARG L   1     1555   1555  1.33  
LINK         C   PHE L   2                 N   LE1 L   3     1555   1555  1.33  
LINK         C   LE1 L   3                 N   THR L   4     1555   1555  1.33  
LINK         C   GLY L   8                 N   SAR L   9     1555   1555  1.34  
LINK         C   SAR L   9                 N   MLE L  10     1555   1555  1.33  
LINK         C   MLE L  10                 N   TYR L  11     1555   1555  1.33  
LINK         C   CYS L  13                 N   NH2 L  14     1555   1555  1.36  
CISPEP   1 GLY A   86    PRO A   87          1        -5.48                     
CISPEP   2 TYR A  204    PRO A  205          1         1.02                     
CISPEP   3 HIS B   31    PRO B   32          1        -1.86                     
CISPEP   4 GLY C   86    PRO C   87          1       -15.41                     
CISPEP   5 TYR C  204    PRO C  205          1         2.82                     
CISPEP   6 HIS D   31    PRO D   32          1         1.98                     
CISPEP   7 GLY E   86    PRO E   87          1       -14.74                     
CISPEP   8 TYR E  204    PRO E  205          1         1.95                     
CISPEP   9 HIS F   31    PRO F   32          1         5.96                     
CISPEP  10 GLY G   86    PRO G   87          1       -10.98                     
CISPEP  11 TYR G  204    PRO G  205          1         1.49                     
CISPEP  12 HIS H   31    PRO H   32          1        -1.22                     
CRYST1  114.320  118.300  248.330  90.00  90.00  90.00 C 2 2 21     32          
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      0.008747  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004027        0.00000                         
MODEL        1                                                                  
HETATM    1  C   ACE K   0      38.805  32.214  11.248  1.00 36.68           C  
HETATM    2  O   ACE K   0      39.117  32.449  12.420  1.00 36.91           O  
HETATM    3  CH3 ACE K   0      38.799  30.814  10.703  1.00 36.59           C  
ATOM      4  N   ARG K   1      38.425  33.169  10.397  1.00 36.48           N  
ATOM      5  CA  ARG K   1      37.999  34.482  10.877  1.00 36.39           C  
ATOM      6  C   ARG K   1      36.486  34.651  10.901  1.00 36.20           C  
ATOM      7  O   ARG K   1      35.757  33.964  10.181  1.00 36.40           O  
ATOM      8  CB  ARG K   1      38.680  35.619  10.103  1.00 36.64           C  
ATOM      9  CG  ARG K   1      39.940  36.150  10.795  1.00 36.95           C  
ATOM     10  CD  ARG K   1      41.217  35.491  10.287  1.00 37.61           C  
ATOM     11  NE  ARG K   1      41.983  36.406   9.442  1.00 38.03           N  
ATOM     12  CZ  ARG K   1      43.143  36.116   8.858  1.00 38.08           C  
ATOM     13  NH1 ARG K   1      43.698  34.918   8.999  1.00 38.09           N  
ATOM     14  NH2 ARG K   1      43.748  37.032   8.121  1.00 38.31           N  
ATOM     15  N   PHE K   2      36.031  35.570  11.748  1.00 35.78           N  
ATOM     16  CA  PHE K   2      34.618  35.723  12.065  1.00 35.53           C  
ATOM     17  C   PHE K   2      34.176  37.177  11.944  1.00 34.76           C  
ATOM     18  O   PHE K   2      34.915  38.091  12.307  1.00 35.11           O  
ATOM     19  CB  PHE K   2      34.342  35.210  13.484  1.00 35.72           C  
ATOM     20  CG  PHE K   2      34.318  33.704  13.603  1.00 36.14           C  
ATOM     21  CD1 PHE K   2      33.129  33.039  13.887  1.00 36.39           C  
ATOM     22  CD2 PHE K   2      35.483  32.950  13.448  1.00 36.47           C  
ATOM     23  CE1 PHE K   2      33.098  31.649  14.005  1.00 36.46           C  
ATOM     24  CE2 PHE K   2      35.461  31.561  13.559  1.00 36.18           C  
ATOM     25  CZ  PHE K   2      34.268  30.910  13.841  1.00 36.23           C  
HETATM   26  O   LE1 K   3      30.802  38.307  13.058  1.00 31.39           O  
HETATM   27  C   LE1 K   3      31.320  39.274  12.520  1.00 31.63           C  
HETATM   28  CA  LE1 K   3      32.358  39.065  11.432  1.00 31.75           C  
HETATM   29  N   LE1 K   3      32.994  37.736  11.697  1.00 32.62           N  
HETATM   30  CB  LE1 K   3      31.822  39.188   9.989  1.00 31.83           C  
HETATM   31  C9  LE1 K   3      30.703  38.199   9.652  1.00 31.09           C  
HETATM   32  C8  LE1 K   3      31.246  40.579   9.699  1.00 31.38           C  
HETATM   33  SG  LE1 K   3      33.159  38.968   8.818  1.00 31.71           S  
ATOM     34  N   THR K   4      31.403  40.482  13.080  1.00 31.57           N  
ATOM     35  CA  THR K   4      30.334  40.912  13.977  1.00 31.99           C  
ATOM     36  C   THR K   4      29.010  41.031  13.233  1.00 32.07           C  
ATOM     37  O   THR K   4      28.960  41.555  12.118  1.00 32.21           O  
ATOM     38  CB  THR K   4      30.646  42.258  14.682  1.00 31.94           C  
ATOM     39  OG1 THR K   4      30.945  43.264  13.707  1.00 32.37           O  
ATOM     40  CG2 THR K   4      31.820  42.117  15.639  1.00 32.04           C  
ATOM     41  N   GLY K   5      27.944  40.535  13.858  1.00 32.07           N  
ATOM     42  CA  GLY K   5      26.597  40.647  13.305  1.00 32.02           C  
ATOM     43  C   GLY K   5      26.058  42.063  13.389  1.00 32.19           C  
ATOM     44  O   GLY K   5      26.675  42.941  14.002  1.00 32.15           O  
ATOM     45  N   HIS K   6      24.903  42.289  12.768  1.00 32.26           N  
ATOM     46  CA  HIS K   6      24.234  43.586  12.845  1.00 32.34           C  
ATOM     47  C   HIS K   6      23.863  43.929  14.290  1.00 32.32           C  
ATOM     48  O   HIS K   6      23.851  45.100  14.669  1.00 32.40           O  
ATOM     49  CB  HIS K   6      22.995  43.614  11.944  1.00 32.38           C  
ATOM     50  CG  HIS K   6      22.242  44.909  11.989  1.00 32.64           C  
ATOM     51  ND1 HIS K   6      22.715  46.068  11.412  1.00 32.54           N  
ATOM     52  CD2 HIS K   6      21.049  45.228  12.548  1.00 32.67           C  
ATOM     53  CE1 HIS K   6      21.847  47.044  11.612  1.00 32.67           C  
ATOM     54  NE2 HIS K   6      20.826  46.560  12.297  1.00 32.27           N  
ATOM     55  N   PHE K   7      23.569  42.903  15.089  1.00 32.31           N  
ATOM     56  CA  PHE K   7      23.254  43.095  16.508  1.00 32.34           C  
ATOM     57  C   PHE K   7      24.394  42.666  17.441  1.00 32.35           C  
ATOM     58  O   PHE K   7      24.240  42.682  18.663  1.00 32.33           O  
ATOM     59  CB  PHE K   7      21.935  42.397  16.877  1.00 32.09           C  
ATOM     60  CG  PHE K   7      20.748  42.909  16.112  1.00 31.74           C  
ATOM     61  CD1 PHE K   7      20.267  44.200  16.327  1.00 31.71           C  
ATOM     62  CD2 PHE K   7      20.116  42.108  15.166  1.00 31.41           C  
ATOM     63  CE1 PHE K   7      19.171  44.681  15.612  1.00 31.54           C  
ATOM     64  CE2 PHE K   7      19.020  42.580  14.447  1.00 30.89           C  
ATOM     65  CZ  PHE K   7      18.549  43.867  14.670  1.00 31.47           C  
ATOM     66  N   GLY K   8      25.535  42.306  16.854  1.00 32.47           N  
ATOM     67  CA  GLY K   8      26.711  41.877  17.610  1.00 32.33           C  
ATOM     68  C   GLY K   8      26.918  40.371  17.586  1.00 32.47           C  
ATOM     69  O   GLY K   8      26.138  39.643  16.963  1.00 32.51           O  
HETATM   70  N   SAR K   9      27.968  39.899  18.264  1.00 32.49           N  
HETATM   71  CA  SAR K   9      28.305  38.473  18.236  1.00 32.56           C  
HETATM   72  C   SAR K   9      29.138  38.083  17.032  1.00 32.86           C  
HETATM   73  O   SAR K   9      29.301  38.894  16.116  1.00 32.96           O  
HETATM   74  CN  SAR K   9      28.835  40.744  19.069  1.00 32.27           C  
HETATM   75  N   MLE K  10      29.671  36.858  17.024  1.00 32.99           N  
HETATM   76  CN  MLE K  10      29.327  35.857  18.033  1.00 33.03           C  
HETATM   77  CA  MLE K  10      30.642  36.482  15.980  1.00 33.05           C  
HETATM   78  CB  MLE K  10      32.013  36.070  16.535  1.00 33.16           C  
HETATM   79  CG  MLE K  10      32.762  37.195  17.261  1.00 33.21           C  
HETATM   80  CD1 MLE K  10      34.153  36.729  17.670  1.00 32.48           C  
HETATM   81  CD2 MLE K  10      32.847  38.488  16.451  1.00 33.02           C  
HETATM   82  C   MLE K  10      30.123  35.449  15.019  1.00 33.38           C  
HETATM   83  O   MLE K  10      29.712  34.359  15.433  1.00 33.20           O  
ATOM     84  N   TYR K  11      30.156  35.779  13.729  1.00 33.58           N  
ATOM     85  CA  TYR K  11      29.606  34.911  12.689  1.00 33.77           C  
ATOM     86  C   TYR K  11      30.650  34.599  11.610  1.00 33.87           C  
ATOM     87  O   TYR K  11      31.434  35.474  11.245  1.00 33.80           O  
ATOM     88  CB  TYR K  11      28.345  35.545  12.090  1.00 33.88           C  
ATOM     89  CG  TYR K  11      27.259  35.801  13.119  1.00 34.15           C  
ATOM     90  CD1 TYR K  11      26.279  34.844  13.377  1.00 33.99           C  
ATOM     91  CD2 TYR K  11      27.225  36.995  13.851  1.00 34.13           C  
ATOM     92  CE1 TYR K  11      25.288  35.070  14.327  1.00 34.19           C  
ATOM     93  CE2 TYR K  11      26.239  37.227  14.803  1.00 33.88           C  
ATOM     94  CZ  TYR K  11      25.274  36.261  15.034  1.00 34.02           C  
ATOM     95  OH  TYR K  11      24.295  36.481  15.974  1.00 34.06           O  
ATOM     96  N   PRO K  12      30.666  33.347  11.105  1.00 34.10           N  
ATOM     97  CA  PRO K  12      31.704  32.875  10.177  1.00 34.20           C  
ATOM     98  C   PRO K  12      31.724  33.641   8.856  1.00 34.35           C  
ATOM     99  O   PRO K  12      30.666  33.886   8.273  1.00 34.73           O  
ATOM    100  CB  PRO K  12      31.318  31.411   9.923  1.00 34.21           C  
ATOM    101  CG  PRO K  12      30.404  31.039  11.045  1.00 34.19           C  
ATOM    102  CD  PRO K  12      29.675  32.292  11.395  1.00 34.18           C  
ATOM    103  N   CYS K  13      32.922  34.010   8.399  1.00 34.21           N  
ATOM    104  CA  CYS K  13      33.100  34.759   7.149  1.00 33.93           C  
ATOM    105  C   CYS K  13      34.530  34.628   6.613  1.00 34.15           C  
ATOM    106  O   CYS K  13      35.050  35.529   5.942  1.00 33.90           O  
ATOM    107  CB  CYS K  13      32.753  36.234   7.356  1.00 33.54           C  
ATOM    108  SG  CYS K  13      33.752  37.033   8.632  1.00 32.61           S  
HETATM  109  N   NH2 K  14      35.117  33.421   6.410  1.00 34.43           N  
TER     110      NH2 K  14                                                      
ENDMDL                                                                          
MASTER        0    0    0   30  120    0    0    611581   12    0  124          
END                                                                             
