GenomeNet

Database: PDB
Entry: 6Q2R
LinkDB: 6Q2R
Original site: 6Q2R 
HEADER    SIGNALING PROTEIN                       08-AUG-19   6Q2R              
TITLE     CRYO-EM STRUCTURE OF RET/GFRA2/NRTN EXTRACELLULAR COMPLEX IN THE      
TITLE    2 TETRAMERIC FORM                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEURTURIN;                                                 
COMPND   3 CHAIN: A, B, U, V;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: GDNF FAMILY RECEPTOR ALPHA-2;                              
COMPND   7 CHAIN: C, D, W, X;                                                   
COMPND   8 SYNONYM: GFR-ALPHA-2,GDNF RECEPTOR BETA,GDNFR-BETA,NEURTURIN RECEPTOR
COMPND   9 ALPHA,NTNR-ALPHA,RET LIGAND 2,TGF-BETA-RELATED NEUROTROPHIC FACTOR   
COMPND  10 RECEPTOR 2;                                                          
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND  14 CHAIN: E, F, Y, Z;                                                   
COMPND  15 SYNONYM: CADHERIN FAMILY MEMBER 12,PROTO-ONCOGENE C-RET;             
COMPND  16 EC: 2.7.10.1;                                                        
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NRTN;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: GFRA2, GDNFRB, RETL2, TRNR2;                                   
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: RET, CDHF12, CDHR16, PTC, RET51;                               
SOURCE  22 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  23 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  25 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    RET, RECEPTOR TYROSINE KINASE, CRYO-EM, SIGNALING PROTEIN             
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.LI,G.J.SHANG,Y.J.CHEN,C.A.BRAUTIGAM,J.LIOU,X.W.ZHANG,X.C.BAI        
REVDAT   2   29-JUL-20 6Q2R    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE                                     
REVDAT   1   02-OCT-19 6Q2R    0                                                
JRNL        AUTH   J.LI,G.SHANG,Y.J.CHEN,C.A.BRAUTIGAM,J.LIOU,X.ZHANG,X.C.BAI   
JRNL        TITL   CRYO-EM ANALYSES REVEAL THE COMMON MECHANISM AND             
JRNL        TITL 2 DIVERSIFICATION IN THE ACTIVATION OF RET BY DIFFERENT        
JRNL        TITL 3 LIGANDS.                                                     
JRNL        REF    ELIFE                         V.   8       2019              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   31535977                                                     
JRNL        DOI    10.7554/ELIFE.47650                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, EPU, RELION, COOT, PHENIX,        
REMARK   3                            RELION, RELION, RELION, RELION            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : 190.000                             
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.300                          
REMARK   3   NUMBER OF PARTICLES               : 15957                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6Q2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243542.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : RET, GFRAL AND GDF15              
REMARK 245                                    EXTRACELLULAR COMPLEX             
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 QUANTUM (4K X 4K)     
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 50.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : 46729                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, F, U, V, W, Y,         
REMARK 350                    AND CHAINS: X, Z                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    96                                                      
REMARK 465     ARG A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     GLY A    99                                                      
REMARK 465     ALA B    96                                                      
REMARK 465     ARG B    97                                                      
REMARK 465     LEU B    98                                                      
REMARK 465     GLY B    99                                                      
REMARK 465     SER C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     GLN C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     GLU C    30                                                      
REMARK 465     LEU C    31                                                      
REMARK 465     HIS C    32                                                      
REMARK 465     GLY C    33                                                      
REMARK 465     TRP C    34                                                      
REMARK 465     ARG C    35                                                      
REMARK 465     PRO C    36                                                      
REMARK 465     GLY C    66                                                      
REMARK 465     ARG C    67                                                      
REMARK 465     ASP C    68                                                      
REMARK 465     ARG C    69                                                      
REMARK 465     ASN C    70                                                      
REMARK 465     THR C    71                                                      
REMARK 465     MET C    72                                                      
REMARK 465     LEU C    73                                                      
REMARK 465     ALA C    74                                                      
REMARK 465     LEU C   116                                                      
REMARK 465     THR C   117                                                      
REMARK 465     GLU C   118                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     GLU C   120                                                      
REMARK 465     THR C   132                                                      
REMARK 465     SER C   133                                                      
REMARK 465     ARG C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     SER C   136                                                      
REMARK 465     ASP C   137                                                      
REMARK 465     ILE C   138                                                      
REMARK 465     PHE C   139                                                      
REMARK 465     ARG C   140                                                      
REMARK 465     LEU C   141                                                      
REMARK 465     ALA C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     ILE C   144                                                      
REMARK 465     PHE C   145                                                      
REMARK 465     SER C   146                                                      
REMARK 465     GLY C   147                                                      
REMARK 465     THR C   148                                                      
REMARK 465     GLY C   149                                                      
REMARK 465     ALA C   150                                                      
REMARK 465     ASP C   151                                                      
REMARK 465     PRO C   152                                                      
REMARK 465     VAL C   153                                                      
REMARK 465     VAL C   154                                                      
REMARK 465     SER C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     LYS C   157                                                      
REMARK 465     SER C   158                                                      
REMARK 465     GLY C   358                                                      
REMARK 465     THR C   359                                                      
REMARK 465     ASP C   360                                                      
REMARK 465     VAL C   361                                                      
REMARK 465     ASN C   362                                                      
REMARK 465     GLY C   363                                                      
REMARK 465     THR C   364                                                      
REMARK 465     HIS C   365                                                      
REMARK 465     HIS C   366                                                      
REMARK 465     HIS C   367                                                      
REMARK 465     HIS C   368                                                      
REMARK 465     HIS C   369                                                      
REMARK 465     HIS C   370                                                      
REMARK 465     HIS C   371                                                      
REMARK 465     HIS C   372                                                      
REMARK 465     PRO E   129                                                      
REMARK 465     THR E   130                                                      
REMARK 465     SER E   131                                                      
REMARK 465     LEU E   132                                                      
REMARK 465     ARG E   133                                                      
REMARK 465     GLU E   134                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     GLU E   136                                                      
REMARK 465     GLU E   208                                                      
REMARK 465     GLY E   209                                                      
REMARK 465     GLU E   210                                                      
REMARK 465     ALA E   247                                                      
REMARK 465     GLY E   248                                                      
REMARK 465     ALA E   249                                                      
REMARK 465     ARG E   250                                                      
REMARK 465     ASP E   380                                                      
REMARK 465     PHE E   381                                                      
REMARK 465     GLN E   382                                                      
REMARK 465     GLY E   383                                                      
REMARK 465     PRO E   384                                                      
REMARK 465     GLY E   385                                                      
REMARK 465     ALA E   386                                                      
REMARK 465     GLU E   623                                                      
REMARK 465     ASP E   624                                                      
REMARK 465     ILE E   625                                                      
REMARK 465     GLN E   626                                                      
REMARK 465     ASP E   627                                                      
REMARK 465     PRO E   628                                                      
REMARK 465     LEU E   629                                                      
REMARK 465     CYS E   630                                                      
REMARK 465     ASP E   631                                                      
REMARK 465     GLU E   632                                                      
REMARK 465     LEU E   633                                                      
REMARK 465     CYS E   634                                                      
REMARK 465     ARG E   635                                                      
REMARK 465     GLY E   636                                                      
REMARK 465     THR E   637                                                      
REMARK 465     HIS E   638                                                      
REMARK 465     HIS E   639                                                      
REMARK 465     HIS E   640                                                      
REMARK 465     HIS E   641                                                      
REMARK 465     HIS E   642                                                      
REMARK 465     HIS E   643                                                      
REMARK 465     HIS E   644                                                      
REMARK 465     HIS E   645                                                      
REMARK 465     SER D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     LEU D    26                                                      
REMARK 465     GLN D    27                                                      
REMARK 465     GLY D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     GLU D    30                                                      
REMARK 465     LEU D    31                                                      
REMARK 465     HIS D    32                                                      
REMARK 465     GLY D    33                                                      
REMARK 465     TRP D    34                                                      
REMARK 465     ARG D    35                                                      
REMARK 465     PRO D    36                                                      
REMARK 465     GLY D    66                                                      
REMARK 465     ARG D    67                                                      
REMARK 465     ASP D    68                                                      
REMARK 465     ARG D    69                                                      
REMARK 465     ASN D    70                                                      
REMARK 465     THR D    71                                                      
REMARK 465     MET D    72                                                      
REMARK 465     LEU D    73                                                      
REMARK 465     ALA D    74                                                      
REMARK 465     LEU D   116                                                      
REMARK 465     THR D   117                                                      
REMARK 465     GLU D   118                                                      
REMARK 465     GLY D   119                                                      
REMARK 465     GLU D   120                                                      
REMARK 465     THR D   132                                                      
REMARK 465     SER D   133                                                      
REMARK 465     ARG D   134                                                      
REMARK 465     LEU D   135                                                      
REMARK 465     SER D   136                                                      
REMARK 465     ASP D   137                                                      
REMARK 465     ILE D   138                                                      
REMARK 465     PHE D   139                                                      
REMARK 465     ARG D   140                                                      
REMARK 465     LEU D   141                                                      
REMARK 465     ALA D   142                                                      
REMARK 465     SER D   143                                                      
REMARK 465     ILE D   144                                                      
REMARK 465     PHE D   145                                                      
REMARK 465     SER D   146                                                      
REMARK 465     GLY D   147                                                      
REMARK 465     THR D   148                                                      
REMARK 465     GLY D   149                                                      
REMARK 465     ALA D   150                                                      
REMARK 465     ASP D   151                                                      
REMARK 465     PRO D   152                                                      
REMARK 465     VAL D   153                                                      
REMARK 465     VAL D   154                                                      
REMARK 465     SER D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     LYS D   157                                                      
REMARK 465     SER D   158                                                      
REMARK 465     GLY D   358                                                      
REMARK 465     THR D   359                                                      
REMARK 465     ASP D   360                                                      
REMARK 465     VAL D   361                                                      
REMARK 465     ASN D   362                                                      
REMARK 465     GLY D   363                                                      
REMARK 465     THR D   364                                                      
REMARK 465     HIS D   365                                                      
REMARK 465     HIS D   366                                                      
REMARK 465     HIS D   367                                                      
REMARK 465     HIS D   368                                                      
REMARK 465     HIS D   369                                                      
REMARK 465     HIS D   370                                                      
REMARK 465     HIS D   371                                                      
REMARK 465     HIS D   372                                                      
REMARK 465     PRO F   129                                                      
REMARK 465     THR F   130                                                      
REMARK 465     SER F   131                                                      
REMARK 465     LEU F   132                                                      
REMARK 465     ARG F   133                                                      
REMARK 465     GLU F   134                                                      
REMARK 465     GLY F   135                                                      
REMARK 465     GLU F   136                                                      
REMARK 465     GLU F   208                                                      
REMARK 465     GLY F   209                                                      
REMARK 465     GLU F   210                                                      
REMARK 465     ALA F   247                                                      
REMARK 465     GLY F   248                                                      
REMARK 465     ALA F   249                                                      
REMARK 465     ARG F   250                                                      
REMARK 465     ASP F   380                                                      
REMARK 465     PHE F   381                                                      
REMARK 465     GLN F   382                                                      
REMARK 465     GLY F   383                                                      
REMARK 465     PRO F   384                                                      
REMARK 465     GLY F   385                                                      
REMARK 465     ALA F   386                                                      
REMARK 465     GLU F   623                                                      
REMARK 465     ASP F   624                                                      
REMARK 465     ILE F   625                                                      
REMARK 465     GLN F   626                                                      
REMARK 465     ASP F   627                                                      
REMARK 465     PRO F   628                                                      
REMARK 465     LEU F   629                                                      
REMARK 465     CYS F   630                                                      
REMARK 465     ASP F   631                                                      
REMARK 465     GLU F   632                                                      
REMARK 465     LEU F   633                                                      
REMARK 465     CYS F   634                                                      
REMARK 465     ARG F   635                                                      
REMARK 465     GLY F   636                                                      
REMARK 465     THR F   637                                                      
REMARK 465     HIS F   638                                                      
REMARK 465     HIS F   639                                                      
REMARK 465     HIS F   640                                                      
REMARK 465     HIS F   641                                                      
REMARK 465     HIS F   642                                                      
REMARK 465     HIS F   643                                                      
REMARK 465     HIS F   644                                                      
REMARK 465     HIS F   645                                                      
REMARK 465     ALA U    96                                                      
REMARK 465     ARG U    97                                                      
REMARK 465     LEU U    98                                                      
REMARK 465     GLY U    99                                                      
REMARK 465     ALA V    96                                                      
REMARK 465     ARG V    97                                                      
REMARK 465     LEU V    98                                                      
REMARK 465     GLY V    99                                                      
REMARK 465     SER W    24                                                      
REMARK 465     SER W    25                                                      
REMARK 465     LEU W    26                                                      
REMARK 465     GLN W    27                                                      
REMARK 465     GLY W    28                                                      
REMARK 465     PRO W    29                                                      
REMARK 465     GLU W    30                                                      
REMARK 465     LEU W    31                                                      
REMARK 465     HIS W    32                                                      
REMARK 465     GLY W    33                                                      
REMARK 465     TRP W    34                                                      
REMARK 465     ARG W    35                                                      
REMARK 465     PRO W    36                                                      
REMARK 465     GLY W    66                                                      
REMARK 465     ARG W    67                                                      
REMARK 465     ASP W    68                                                      
REMARK 465     ARG W    69                                                      
REMARK 465     ASN W    70                                                      
REMARK 465     THR W    71                                                      
REMARK 465     MET W    72                                                      
REMARK 465     LEU W    73                                                      
REMARK 465     ALA W    74                                                      
REMARK 465     LEU W   116                                                      
REMARK 465     THR W   117                                                      
REMARK 465     GLU W   118                                                      
REMARK 465     GLY W   119                                                      
REMARK 465     GLU W   120                                                      
REMARK 465     THR W   132                                                      
REMARK 465     SER W   133                                                      
REMARK 465     ARG W   134                                                      
REMARK 465     LEU W   135                                                      
REMARK 465     SER W   136                                                      
REMARK 465     ASP W   137                                                      
REMARK 465     ILE W   138                                                      
REMARK 465     PHE W   139                                                      
REMARK 465     ARG W   140                                                      
REMARK 465     LEU W   141                                                      
REMARK 465     ALA W   142                                                      
REMARK 465     SER W   143                                                      
REMARK 465     ILE W   144                                                      
REMARK 465     PHE W   145                                                      
REMARK 465     SER W   146                                                      
REMARK 465     GLY W   147                                                      
REMARK 465     THR W   148                                                      
REMARK 465     GLY W   149                                                      
REMARK 465     ALA W   150                                                      
REMARK 465     ASP W   151                                                      
REMARK 465     PRO W   152                                                      
REMARK 465     VAL W   153                                                      
REMARK 465     VAL W   154                                                      
REMARK 465     SER W   155                                                      
REMARK 465     ALA W   156                                                      
REMARK 465     LYS W   157                                                      
REMARK 465     SER W   158                                                      
REMARK 465     GLY W   358                                                      
REMARK 465     THR W   359                                                      
REMARK 465     ASP W   360                                                      
REMARK 465     VAL W   361                                                      
REMARK 465     ASN W   362                                                      
REMARK 465     GLY W   363                                                      
REMARK 465     THR W   364                                                      
REMARK 465     HIS W   365                                                      
REMARK 465     HIS W   366                                                      
REMARK 465     HIS W   367                                                      
REMARK 465     HIS W   368                                                      
REMARK 465     HIS W   369                                                      
REMARK 465     HIS W   370                                                      
REMARK 465     HIS W   371                                                      
REMARK 465     HIS W   372                                                      
REMARK 465     PRO Y   129                                                      
REMARK 465     THR Y   130                                                      
REMARK 465     SER Y   131                                                      
REMARK 465     LEU Y   132                                                      
REMARK 465     ARG Y   133                                                      
REMARK 465     GLU Y   134                                                      
REMARK 465     GLY Y   135                                                      
REMARK 465     GLU Y   136                                                      
REMARK 465     GLU Y   208                                                      
REMARK 465     GLY Y   209                                                      
REMARK 465     GLU Y   210                                                      
REMARK 465     ALA Y   247                                                      
REMARK 465     GLY Y   248                                                      
REMARK 465     ALA Y   249                                                      
REMARK 465     ARG Y   250                                                      
REMARK 465     ASP Y   380                                                      
REMARK 465     PHE Y   381                                                      
REMARK 465     GLN Y   382                                                      
REMARK 465     GLY Y   383                                                      
REMARK 465     PRO Y   384                                                      
REMARK 465     GLY Y   385                                                      
REMARK 465     ALA Y   386                                                      
REMARK 465     GLU Y   623                                                      
REMARK 465     ASP Y   624                                                      
REMARK 465     ILE Y   625                                                      
REMARK 465     GLN Y   626                                                      
REMARK 465     ASP Y   627                                                      
REMARK 465     PRO Y   628                                                      
REMARK 465     LEU Y   629                                                      
REMARK 465     CYS Y   630                                                      
REMARK 465     ASP Y   631                                                      
REMARK 465     GLU Y   632                                                      
REMARK 465     LEU Y   633                                                      
REMARK 465     CYS Y   634                                                      
REMARK 465     ARG Y   635                                                      
REMARK 465     GLY Y   636                                                      
REMARK 465     THR Y   637                                                      
REMARK 465     HIS Y   638                                                      
REMARK 465     HIS Y   639                                                      
REMARK 465     HIS Y   640                                                      
REMARK 465     HIS Y   641                                                      
REMARK 465     HIS Y   642                                                      
REMARK 465     HIS Y   643                                                      
REMARK 465     HIS Y   644                                                      
REMARK 465     HIS Y   645                                                      
REMARK 465     SER X    24                                                      
REMARK 465     SER X    25                                                      
REMARK 465     LEU X    26                                                      
REMARK 465     GLN X    27                                                      
REMARK 465     GLY X    28                                                      
REMARK 465     PRO X    29                                                      
REMARK 465     GLU X    30                                                      
REMARK 465     LEU X    31                                                      
REMARK 465     HIS X    32                                                      
REMARK 465     GLY X    33                                                      
REMARK 465     TRP X    34                                                      
REMARK 465     ARG X    35                                                      
REMARK 465     PRO X    36                                                      
REMARK 465     GLY X    66                                                      
REMARK 465     ARG X    67                                                      
REMARK 465     ASP X    68                                                      
REMARK 465     ARG X    69                                                      
REMARK 465     ASN X    70                                                      
REMARK 465     THR X    71                                                      
REMARK 465     MET X    72                                                      
REMARK 465     LEU X    73                                                      
REMARK 465     ALA X    74                                                      
REMARK 465     LEU X   116                                                      
REMARK 465     THR X   117                                                      
REMARK 465     GLU X   118                                                      
REMARK 465     GLY X   119                                                      
REMARK 465     GLU X   120                                                      
REMARK 465     THR X   132                                                      
REMARK 465     SER X   133                                                      
REMARK 465     ARG X   134                                                      
REMARK 465     LEU X   135                                                      
REMARK 465     SER X   136                                                      
REMARK 465     ASP X   137                                                      
REMARK 465     ILE X   138                                                      
REMARK 465     PHE X   139                                                      
REMARK 465     ARG X   140                                                      
REMARK 465     LEU X   141                                                      
REMARK 465     ALA X   142                                                      
REMARK 465     SER X   143                                                      
REMARK 465     ILE X   144                                                      
REMARK 465     PHE X   145                                                      
REMARK 465     SER X   146                                                      
REMARK 465     GLY X   147                                                      
REMARK 465     THR X   148                                                      
REMARK 465     GLY X   149                                                      
REMARK 465     ALA X   150                                                      
REMARK 465     ASP X   151                                                      
REMARK 465     PRO X   152                                                      
REMARK 465     VAL X   153                                                      
REMARK 465     VAL X   154                                                      
REMARK 465     SER X   155                                                      
REMARK 465     ALA X   156                                                      
REMARK 465     LYS X   157                                                      
REMARK 465     SER X   158                                                      
REMARK 465     GLY X   358                                                      
REMARK 465     THR X   359                                                      
REMARK 465     ASP X   360                                                      
REMARK 465     VAL X   361                                                      
REMARK 465     ASN X   362                                                      
REMARK 465     GLY X   363                                                      
REMARK 465     THR X   364                                                      
REMARK 465     HIS X   365                                                      
REMARK 465     HIS X   366                                                      
REMARK 465     HIS X   367                                                      
REMARK 465     HIS X   368                                                      
REMARK 465     HIS X   369                                                      
REMARK 465     HIS X   370                                                      
REMARK 465     HIS X   371                                                      
REMARK 465     HIS X   372                                                      
REMARK 465     PRO Z   129                                                      
REMARK 465     THR Z   130                                                      
REMARK 465     SER Z   131                                                      
REMARK 465     LEU Z   132                                                      
REMARK 465     ARG Z   133                                                      
REMARK 465     GLU Z   134                                                      
REMARK 465     GLY Z   135                                                      
REMARK 465     GLU Z   136                                                      
REMARK 465     GLU Z   208                                                      
REMARK 465     GLY Z   209                                                      
REMARK 465     GLU Z   210                                                      
REMARK 465     ALA Z   247                                                      
REMARK 465     GLY Z   248                                                      
REMARK 465     ALA Z   249                                                      
REMARK 465     ARG Z   250                                                      
REMARK 465     ASP Z   380                                                      
REMARK 465     PHE Z   381                                                      
REMARK 465     GLN Z   382                                                      
REMARK 465     GLY Z   383                                                      
REMARK 465     PRO Z   384                                                      
REMARK 465     GLY Z   385                                                      
REMARK 465     ALA Z   386                                                      
REMARK 465     GLU Z   623                                                      
REMARK 465     ASP Z   624                                                      
REMARK 465     ILE Z   625                                                      
REMARK 465     GLN Z   626                                                      
REMARK 465     ASP Z   627                                                      
REMARK 465     PRO Z   628                                                      
REMARK 465     LEU Z   629                                                      
REMARK 465     CYS Z   630                                                      
REMARK 465     ASP Z   631                                                      
REMARK 465     GLU Z   632                                                      
REMARK 465     LEU Z   633                                                      
REMARK 465     CYS Z   634                                                      
REMARK 465     ARG Z   635                                                      
REMARK 465     GLY Z   636                                                      
REMARK 465     THR Z   637                                                      
REMARK 465     HIS Z   638                                                      
REMARK 465     HIS Z   639                                                      
REMARK 465     HIS Z   640                                                      
REMARK 465     HIS Z   641                                                      
REMARK 465     HIS Z   642                                                      
REMARK 465     HIS Z   643                                                      
REMARK 465     HIS Z   644                                                      
REMARK 465     HIS Z   645                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP F   300     OH   TYR F   314              1.38            
REMARK 500   OD2  ASP Y   300     OH   TYR Y   314              1.38            
REMARK 500   OD2  ASP Z   300     OH   TYR Z   314              1.38            
REMARK 500   OD2  ASP E   300     OH   TYR E   314              1.38            
REMARK 500   OD1  ASP Y   230     OE1  GLU Y   232              1.70            
REMARK 500   OD1  ASP Z   230     OE1  GLU Z   232              1.70            
REMARK 500   OD1  ASP E   230     OE1  GLU E   232              1.70            
REMARK 500   OD1  ASP F   230     OE1  GLU F   232              1.70            
REMARK 500   OE1  GLU Z   178     OD1  ASP Z   230              1.71            
REMARK 500   OE1  GLU E   178     OD1  ASP E   230              1.71            
REMARK 500   OE1  GLU F   178     OD1  ASP F   230              1.71            
REMARK 500   OE1  GLU Y   178     OD1  ASP Y   230              1.71            
REMARK 500   OD1  ASP Z   266     OD2  ASP Z   302              1.76            
REMARK 500   OD1  ASP F   266     OD2  ASP F   302              1.76            
REMARK 500   OD1  ASP Y   266     OD2  ASP Y   302              1.76            
REMARK 500   OD1  ASP E   266     OD2  ASP E   302              1.76            
REMARK 500   OE1  GLU Z   178     OE1  GLU Z   232              2.00            
REMARK 500   OE1  GLU E   178     OE1  GLU E   232              2.00            
REMARK 500   OE1  GLU F   178     OE1  GLU F   232              2.00            
REMARK 500   OE1  GLU Y   178     OE1  GLU Y   232              2.00            
REMARK 500   OD1  ASP E   567     OD2  ASP E   584              2.03            
REMARK 500   OD1  ASP Z   567     OD2  ASP Z   584              2.03            
REMARK 500   OD1  ASP Y   567     OD2  ASP Y   584              2.03            
REMARK 500   OD1  ASP F   567     OD2  ASP F   584              2.03            
REMARK 500   O    HIS F   569     OD2  ASP F   584              2.03            
REMARK 500   O    HIS E   569     OD2  ASP E   584              2.03            
REMARK 500   O    HIS Z   569     OD2  ASP Z   584              2.03            
REMARK 500   O    HIS Y   569     OD2  ASP Y   584              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG B 192      -30.27   -130.71                                   
REMARK 500    ILE C 189      -62.32   -101.35                                   
REMARK 500    LEU C 238       76.53     54.73                                   
REMARK 500    MET C 305       58.68    -95.70                                   
REMARK 500    MET C 331       30.36    -94.76                                   
REMARK 500    LEU E  50      -60.21    -92.76                                   
REMARK 500    PRO E  60       48.43    -76.72                                   
REMARK 500    GLN E  70       30.13    -92.35                                   
REMARK 500    HIS E 114       62.67     60.34                                   
REMARK 500    SER E 220      115.78   -161.42                                   
REMARK 500    LEU E 221       30.06    -88.47                                   
REMARK 500    PRO E 320     -169.37    -75.12                                   
REMARK 500    ILE E 422      -62.58   -122.38                                   
REMARK 500    LYS E 549       31.79    -99.97                                   
REMARK 500    PRO E 566       43.63    -85.78                                   
REMARK 500    ASN E 579       -7.13   -140.38                                   
REMARK 500    ILE D 189      -62.33   -101.32                                   
REMARK 500    LEU D 238       76.51     54.79                                   
REMARK 500    MET D 305       58.69    -95.73                                   
REMARK 500    MET D 331       30.34    -94.75                                   
REMARK 500    LEU F  50      -60.19    -92.75                                   
REMARK 500    PRO F  60       48.45    -76.69                                   
REMARK 500    GLN F  70       30.13    -92.32                                   
REMARK 500    HIS F 114       62.65     60.32                                   
REMARK 500    SER F 220      115.79   -161.39                                   
REMARK 500    LEU F 221       30.07    -88.47                                   
REMARK 500    PRO F 320     -169.40    -75.05                                   
REMARK 500    ILE F 422      -62.57   -122.36                                   
REMARK 500    LYS F 549       31.74    -99.96                                   
REMARK 500    PRO F 566       43.65    -85.79                                   
REMARK 500    ASN F 579       -7.14   -140.39                                   
REMARK 500    ARG V 192      -30.31   -130.73                                   
REMARK 500    ILE W 189      -62.28   -101.34                                   
REMARK 500    LEU W 238       76.49     54.76                                   
REMARK 500    MET W 305       58.69    -95.71                                   
REMARK 500    MET W 331       30.25    -94.81                                   
REMARK 500    LEU Y  50      -60.16    -92.69                                   
REMARK 500    PRO Y  60       48.48    -76.78                                   
REMARK 500    GLN Y  70       30.02    -92.33                                   
REMARK 500    HIS Y 114       62.59     60.34                                   
REMARK 500    SER Y 220      115.70   -161.45                                   
REMARK 500    LEU Y 221       30.09    -88.39                                   
REMARK 500    PRO Y 320     -169.39    -75.09                                   
REMARK 500    ILE Y 422      -62.52   -122.35                                   
REMARK 500    PRO Y 566       43.62    -85.76                                   
REMARK 500    ASN Y 579       -7.15   -140.41                                   
REMARK 500    ILE X 189      -62.24   -101.37                                   
REMARK 500    LEU X 238       76.50     54.74                                   
REMARK 500    MET X 305       58.71    -95.71                                   
REMARK 500    MET X 331       30.26    -94.77                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 178   OE1                                                    
REMARK 620 2 GLU E 178   OE2  55.1                                              
REMARK 620 3 ASN E 179   OD1 110.9 100.7                                        
REMARK 620 4 ASP E 230   OD1  44.1  98.8 112.1                                  
REMARK 620 5 ASP E 230   OD2 100.0 149.0 106.0  56.7                            
REMARK 620 6 GLU E 232   OE1  49.3  81.5 153.9  42.6  67.6                      
REMARK 620 7 ASP E 267   OD2 104.2  72.8 131.1 116.8 100.1  74.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 232   OE2                                                    
REMARK 620 2 ASP E 264   OD1  64.1                                              
REMARK 620 3 ASP E 264   OD2  88.7  55.6                                        
REMARK 620 4 GLU E 265   O   110.2  64.6  98.5                                  
REMARK 620 5 ASP E 267   OD1  64.6  97.8 149.7  79.3                            
REMARK 620 6 ASP E 302   OD1 134.4 148.3 133.4  83.7  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 266   OD1                                                    
REMARK 620 2 SER E 268   O    90.5                                              
REMARK 620 3 ASP E 300   OD1 135.0  59.5                                        
REMARK 620 4 ASP E 300   OD2 168.8 100.4  51.5                                  
REMARK 620 5 ASP E 302   OD2  41.8  62.6  93.2 142.9                            
REMARK 620 6 TYR E 314   OH  136.4 130.6  85.5  34.5 161.0                      
REMARK 620 7 ASP E 378   OD1  83.1 118.9 139.3  93.8 123.3  65.7                
REMARK 620 8 ASP E 378   OD2 107.6  75.3  96.8  78.1 123.1  75.8  50.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 564   O                                                      
REMARK 620 2 ASP E 567   OD1  82.4                                              
REMARK 620 3 ASP E 567   OD2  73.2  55.5                                        
REMARK 620 4 HIS E 569   O   137.4  65.7  65.7                                  
REMARK 620 5 GLU E 574   OE1 127.7 140.9 147.2  94.0                            
REMARK 620 6 GLU E 574   OE2  73.0 146.0 133.5 146.6  54.8                      
REMARK 620 7 ASP E 584   OD2 126.6  50.8  94.4  49.6  90.4 131.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 178   OE1                                                    
REMARK 620 2 GLU F 178   OE2  55.1                                              
REMARK 620 3 ASN F 179   OD1 110.9 100.7                                        
REMARK 620 4 ASP F 230   OD1  44.1  98.8 112.1                                  
REMARK 620 5 ASP F 230   OD2  99.9 149.0 106.0  56.7                            
REMARK 620 6 GLU F 232   OE1  49.3  81.5 153.9  42.6  67.6                      
REMARK 620 7 ASP F 267   OD2 104.2  72.8 131.1 116.8 100.1  74.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 232   OE2                                                    
REMARK 620 2 ASP F 264   OD1  64.1                                              
REMARK 620 3 ASP F 264   OD2  88.7  55.6                                        
REMARK 620 4 GLU F 265   O   110.3  64.6  98.5                                  
REMARK 620 5 ASP F 267   OD1  64.6  97.8 149.7  79.3                            
REMARK 620 6 ASP F 302   OD1 134.4 148.3 133.4  83.7  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 266   OD1                                                    
REMARK 620 2 SER F 268   O    90.5                                              
REMARK 620 3 ASP F 300   OD1 135.1  59.5                                        
REMARK 620 4 ASP F 300   OD2 168.8 100.4  51.5                                  
REMARK 620 5 ASP F 302   OD2  41.8  62.6  93.2 142.9                            
REMARK 620 6 TYR F 314   OH  136.4 130.6  85.5  34.4 161.0                      
REMARK 620 7 ASP F 378   OD1  83.1 118.9 139.3  93.8 123.3  65.7                
REMARK 620 8 ASP F 378   OD2 107.6  75.3  96.8  78.1 123.1  75.8  50.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR F 564   O                                                      
REMARK 620 2 ASP F 567   OD1  82.4                                              
REMARK 620 3 ASP F 567   OD2  73.2  55.5                                        
REMARK 620 4 HIS F 569   O   137.4  65.7  65.7                                  
REMARK 620 5 GLU F 574   OE1 127.7 141.0 147.2  94.0                            
REMARK 620 6 GLU F 574   OE2  73.0 146.0 133.5 146.6  54.8                      
REMARK 620 7 ASP F 584   OD2 126.6  50.8  94.4  49.6  90.4 131.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU Y 178   OE1                                                    
REMARK 620 2 GLU Y 178   OE2  55.1                                              
REMARK 620 3 ASN Y 179   OD1 110.9 100.7                                        
REMARK 620 4 ASP Y 230   OD1  44.1  98.8 112.1                                  
REMARK 620 5 ASP Y 230   OD2  99.9 148.9 106.1  56.7                            
REMARK 620 6 GLU Y 232   OE1  49.3  81.5 153.9  42.5  67.5                      
REMARK 620 7 ASP Y 267   OD2 104.2  72.7 131.1 116.8 100.0  74.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU Y 232   OE2                                                    
REMARK 620 2 ASP Y 264   OD1  64.1                                              
REMARK 620 3 ASP Y 264   OD2  88.7  55.6                                        
REMARK 620 4 GLU Y 265   O   110.2  64.6  98.5                                  
REMARK 620 5 ASP Y 267   OD1  64.6  97.7 149.7  79.3                            
REMARK 620 6 ASP Y 302   OD1 134.4 148.3 133.4  83.7  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP Y 266   OD1                                                    
REMARK 620 2 SER Y 268   O    90.5                                              
REMARK 620 3 ASP Y 300   OD1 135.0  59.5                                        
REMARK 620 4 ASP Y 300   OD2 168.8 100.4  51.5                                  
REMARK 620 5 ASP Y 302   OD2  41.8  62.7  93.2 142.9                            
REMARK 620 6 TYR Y 314   OH  136.4 130.6  85.5  34.4 161.0                      
REMARK 620 7 ASP Y 378   OD1  83.1 118.9 139.3  93.8 123.3  65.7                
REMARK 620 8 ASP Y 378   OD2 107.6  75.3  96.8  78.1 123.1  75.8  50.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR Y 564   O                                                      
REMARK 620 2 ASP Y 567   OD1  82.4                                              
REMARK 620 3 ASP Y 567   OD2  73.3  55.5                                        
REMARK 620 4 HIS Y 569   O   137.5  65.7  65.7                                  
REMARK 620 5 GLU Y 574   OE1 127.7 140.9 147.2  94.0                            
REMARK 620 6 GLU Y 574   OE2  73.0 146.0 133.5 146.5  54.8                      
REMARK 620 7 ASP Y 584   OD2 126.6  50.8  94.4  49.6  90.4 131.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Z2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU Z 178   OE1                                                    
REMARK 620 2 GLU Z 178   OE2  55.1                                              
REMARK 620 3 ASN Z 179   OD1 110.9 100.7                                        
REMARK 620 4 ASP Z 230   OD1  44.1  98.8 112.1                                  
REMARK 620 5 ASP Z 230   OD2  99.9 149.0 106.1  56.7                            
REMARK 620 6 GLU Z 232   OE1  49.3  81.5 154.0  42.6  67.5                      
REMARK 620 7 ASP Z 267   OD2 104.2  72.7 131.1 116.8 100.0  74.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Z2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU Z 232   OE2                                                    
REMARK 620 2 ASP Z 264   OD1  64.1                                              
REMARK 620 3 ASP Z 264   OD2  88.7  55.7                                        
REMARK 620 4 GLU Z 265   O   110.2  64.6  98.5                                  
REMARK 620 5 ASP Z 267   OD1  64.6  97.7 149.7  79.3                            
REMARK 620 6 ASP Z 302   OD1 134.4 148.3 133.4  83.7  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Z2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP Z 266   OD1                                                    
REMARK 620 2 SER Z 268   O    90.5                                              
REMARK 620 3 ASP Z 300   OD1 135.0  59.5                                        
REMARK 620 4 ASP Z 300   OD2 168.8 100.4  51.5                                  
REMARK 620 5 ASP Z 302   OD2  41.8  62.7  93.3 142.9                            
REMARK 620 6 TYR Z 314   OH  136.4 130.6  85.5  34.5 161.0                      
REMARK 620 7 ASP Z 378   OD1  83.1 118.9 139.3  93.8 123.3  65.7                
REMARK 620 8 ASP Z 378   OD2 107.6  75.3  96.8  78.1 123.1  75.8  50.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Z2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR Z 564   O                                                      
REMARK 620 2 ASP Z 567   OD1  82.4                                              
REMARK 620 3 ASP Z 567   OD2  73.3  55.5                                        
REMARK 620 4 HIS Z 569   O   137.4  65.7  65.7                                  
REMARK 620 5 GLU Z 574   OE1 127.7 140.9 147.2  94.0                            
REMARK 620 6 GLU Z 574   OE2  73.0 146.0 133.6 146.5  54.8                      
REMARK 620 7 ASP Z 584   OD2 126.6  50.8  94.4  49.6  90.4 131.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-20576   RELATED DB: EMDB                             
REMARK 900 RELATED ID: EMD-20577   RELATED DB: EMDB                             
REMARK 900 RELATED ID: EMD-20578   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF RET/GFRA2/NRTN EXTRACELLULAR COMPLEX IN THE     
REMARK 900 TETRAMERIC FORM.                                                     
DBREF  6Q2R A   96   197  UNP    Q99748   NRTN_HUMAN      96    197             
DBREF  6Q2R B   96   197  UNP    Q99748   NRTN_HUMAN      96    197             
DBREF  6Q2R C   24   362  UNP    O00451   GFRA2_HUMAN     24    362             
DBREF  6Q2R E   29   635  UNP    P07949   RET_HUMAN       29    635             
DBREF  6Q2R D   24   362  UNP    O00451   GFRA2_HUMAN     24    362             
DBREF  6Q2R F   29   635  UNP    P07949   RET_HUMAN       29    635             
DBREF  6Q2R U   96   197  UNP    Q99748   NRTN_HUMAN      96    197             
DBREF  6Q2R V   96   197  UNP    Q99748   NRTN_HUMAN      96    197             
DBREF  6Q2R W   24   362  UNP    O00451   GFRA2_HUMAN     24    362             
DBREF  6Q2R Y   29   635  UNP    P07949   RET_HUMAN       29    635             
DBREF  6Q2R X   24   362  UNP    O00451   GFRA2_HUMAN     24    362             
DBREF  6Q2R Z   29   635  UNP    P07949   RET_HUMAN       29    635             
SEQADV 6Q2R GLY C  363  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R THR C  364  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  365  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  366  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  367  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  368  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  369  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  370  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  371  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS C  372  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  114  UNP  P07949    ARG   114 CONFLICT                       
SEQADV 6Q2R GLY E  636  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R THR E  637  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  638  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  639  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  640  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  641  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  642  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  643  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  644  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS E  645  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R GLY D  363  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R THR D  364  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  365  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  366  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  367  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  368  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  369  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  370  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  371  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS D  372  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  114  UNP  P07949    ARG   114 CONFLICT                       
SEQADV 6Q2R GLY F  636  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R THR F  637  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  638  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  639  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  640  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  641  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  642  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  643  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  644  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS F  645  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R GLY W  363  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R THR W  364  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  365  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  366  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  367  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  368  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  369  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  370  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  371  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS W  372  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  114  UNP  P07949    ARG   114 CONFLICT                       
SEQADV 6Q2R GLY Y  636  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R THR Y  637  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  638  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  639  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  640  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  641  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  642  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  643  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  644  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Y  645  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R GLY X  363  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R THR X  364  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  365  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  366  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  367  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  368  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  369  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  370  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  371  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS X  372  UNP  O00451              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  114  UNP  P07949    ARG   114 CONFLICT                       
SEQADV 6Q2R GLY Z  636  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R THR Z  637  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  638  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  639  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  640  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  641  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  642  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  643  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  644  UNP  P07949              EXPRESSION TAG                 
SEQADV 6Q2R HIS Z  645  UNP  P07949              EXPRESSION TAG                 
SEQRES   1 A  102  ALA ARG LEU GLY ALA ARG PRO CYS GLY LEU ARG GLU LEU          
SEQRES   2 A  102  GLU VAL ARG VAL SER GLU LEU GLY LEU GLY TYR ALA SER          
SEQRES   3 A  102  ASP GLU THR VAL LEU PHE ARG TYR CYS ALA GLY ALA CYS          
SEQRES   4 A  102  GLU ALA ALA ALA ARG VAL TYR ASP LEU GLY LEU ARG ARG          
SEQRES   5 A  102  LEU ARG GLN ARG ARG ARG LEU ARG ARG GLU ARG VAL ARG          
SEQRES   6 A  102  ALA GLN PRO CYS CYS ARG PRO THR ALA TYR GLU ASP GLU          
SEQRES   7 A  102  VAL SER PHE LEU ASP ALA HIS SER ARG TYR HIS THR VAL          
SEQRES   8 A  102  HIS GLU LEU SER ALA ARG GLU CYS ALA CYS VAL                  
SEQRES   1 B  102  ALA ARG LEU GLY ALA ARG PRO CYS GLY LEU ARG GLU LEU          
SEQRES   2 B  102  GLU VAL ARG VAL SER GLU LEU GLY LEU GLY TYR ALA SER          
SEQRES   3 B  102  ASP GLU THR VAL LEU PHE ARG TYR CYS ALA GLY ALA CYS          
SEQRES   4 B  102  GLU ALA ALA ALA ARG VAL TYR ASP LEU GLY LEU ARG ARG          
SEQRES   5 B  102  LEU ARG GLN ARG ARG ARG LEU ARG ARG GLU ARG VAL ARG          
SEQRES   6 B  102  ALA GLN PRO CYS CYS ARG PRO THR ALA TYR GLU ASP GLU          
SEQRES   7 B  102  VAL SER PHE LEU ASP ALA HIS SER ARG TYR HIS THR VAL          
SEQRES   8 B  102  HIS GLU LEU SER ALA ARG GLU CYS ALA CYS VAL                  
SEQRES   1 C  349  SER SER LEU GLN GLY PRO GLU LEU HIS GLY TRP ARG PRO          
SEQRES   2 C  349  PRO VAL ASP CYS VAL ARG ALA ASN GLU LEU CYS ALA ALA          
SEQRES   3 C  349  GLU SER ASN CYS SER SER ARG TYR ARG THR LEU ARG GLN          
SEQRES   4 C  349  CYS LEU ALA GLY ARG ASP ARG ASN THR MET LEU ALA ASN          
SEQRES   5 C  349  LYS GLU CYS GLN ALA ALA LEU GLU VAL LEU GLN GLU SER          
SEQRES   6 C  349  PRO LEU TYR ASP CYS ARG CYS LYS ARG GLY MET LYS LYS          
SEQRES   7 C  349  GLU LEU GLN CYS LEU GLN ILE TYR TRP SER ILE HIS LEU          
SEQRES   8 C  349  GLY LEU THR GLU GLY GLU GLU PHE TYR GLU ALA SER PRO          
SEQRES   9 C  349  TYR GLU PRO VAL THR SER ARG LEU SER ASP ILE PHE ARG          
SEQRES  10 C  349  LEU ALA SER ILE PHE SER GLY THR GLY ALA ASP PRO VAL          
SEQRES  11 C  349  VAL SER ALA LYS SER ASN HIS CYS LEU ASP ALA ALA LYS          
SEQRES  12 C  349  ALA CYS ASN LEU ASN ASP ASN CYS LYS LYS LEU ARG SER          
SEQRES  13 C  349  SER TYR ILE SER ILE CYS ASN ARG GLU ILE SER PRO THR          
SEQRES  14 C  349  GLU ARG CYS ASN ARG ARG LYS CYS HIS LYS ALA LEU ARG          
SEQRES  15 C  349  GLN PHE PHE ASP ARG VAL PRO SER GLU TYR THR TYR ARG          
SEQRES  16 C  349  MET LEU PHE CYS SER CYS GLN ASP GLN ALA CYS ALA GLU          
SEQRES  17 C  349  ARG ARG ARG GLN THR ILE LEU PRO SER CYS SER TYR GLU          
SEQRES  18 C  349  ASP LYS GLU LYS PRO ASN CYS LEU ASP LEU ARG GLY VAL          
SEQRES  19 C  349  CYS ARG THR ASP HIS LEU CYS ARG SER ARG LEU ALA ASP          
SEQRES  20 C  349  PHE HIS ALA ASN CYS ARG ALA SER TYR GLN THR VAL THR          
SEQRES  21 C  349  SER CYS PRO ALA ASP ASN TYR GLN ALA CYS LEU GLY SER          
SEQRES  22 C  349  TYR ALA GLY MET ILE GLY PHE ASP MET THR PRO ASN TYR          
SEQRES  23 C  349  VAL ASP SER SER PRO THR GLY ILE VAL VAL SER PRO TRP          
SEQRES  24 C  349  CYS SER CYS ARG GLY SER GLY ASN MET GLU GLU GLU CYS          
SEQRES  25 C  349  GLU LYS PHE LEU ARG ASP PHE THR GLU ASN PRO CYS LEU          
SEQRES  26 C  349  ARG ASN ALA ILE GLN ALA PHE GLY ASN GLY THR ASP VAL          
SEQRES  27 C  349  ASN GLY THR HIS HIS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 E  617  LEU TYR PHE SER ARG ASP ALA TYR TRP GLU LYS LEU TYR          
SEQRES   2 E  617  VAL ASP GLN ALA ALA GLY THR PRO LEU LEU TYR VAL HIS          
SEQRES   3 E  617  ALA LEU ARG ASP ALA PRO GLU GLU VAL PRO SER PHE ARG          
SEQRES   4 E  617  LEU GLY GLN HIS LEU TYR GLY THR TYR ARG THR ARG LEU          
SEQRES   5 E  617  HIS GLU ASN ASN TRP ILE CYS ILE GLN GLU ASP THR GLY          
SEQRES   6 E  617  LEU LEU TYR LEU ASN ARG SER LEU ASP HIS SER SER TRP          
SEQRES   7 E  617  GLU LYS LEU SER VAL ARG ASN HIS GLY PHE PRO LEU LEU          
SEQRES   8 E  617  THR VAL TYR LEU LYS VAL PHE LEU SER PRO THR SER LEU          
SEQRES   9 E  617  ARG GLU GLY GLU CYS GLN TRP PRO GLY CYS ALA ARG VAL          
SEQRES  10 E  617  TYR PHE SER PHE PHE ASN THR SER PHE PRO ALA CYS SER          
SEQRES  11 E  617  SER LEU LYS PRO ARG GLU LEU CYS PHE PRO GLU THR ARG          
SEQRES  12 E  617  PRO SER PHE ARG ILE ARG GLU ASN ARG PRO PRO GLY THR          
SEQRES  13 E  617  PHE HIS GLN PHE ARG LEU LEU PRO VAL GLN PHE LEU CYS          
SEQRES  14 E  617  PRO ASN ILE SER VAL ALA TYR ARG LEU LEU GLU GLY GLU          
SEQRES  15 E  617  GLY LEU PRO PHE ARG CYS ALA PRO ASP SER LEU GLU VAL          
SEQRES  16 E  617  SER THR ARG TRP ALA LEU ASP ARG GLU GLN ARG GLU LYS          
SEQRES  17 E  617  TYR GLU LEU VAL ALA VAL CYS THR VAL HIS ALA GLY ALA          
SEQRES  18 E  617  ARG GLU GLU VAL VAL MET VAL PRO PHE PRO VAL THR VAL          
SEQRES  19 E  617  TYR ASP GLU ASP ASP SER ALA PRO THR PHE PRO ALA GLY          
SEQRES  20 E  617  VAL ASP THR ALA SER ALA VAL VAL GLU PHE LYS ARG LYS          
SEQRES  21 E  617  GLU ASP THR VAL VAL ALA THR LEU ARG VAL PHE ASP ALA          
SEQRES  22 E  617  ASP VAL VAL PRO ALA SER GLY GLU LEU VAL ARG ARG TYR          
SEQRES  23 E  617  THR SER THR LEU LEU PRO GLY ASP THR TRP ALA GLN GLN          
SEQRES  24 E  617  THR PHE ARG VAL GLU HIS TRP PRO ASN GLU THR SER VAL          
SEQRES  25 E  617  GLN ALA ASN GLY SER PHE VAL ARG ALA THR VAL HIS ASP          
SEQRES  26 E  617  TYR ARG LEU VAL LEU ASN ARG ASN LEU SER ILE SER GLU          
SEQRES  27 E  617  ASN ARG THR MET GLN LEU ALA VAL LEU VAL ASN ASP SER          
SEQRES  28 E  617  ASP PHE GLN GLY PRO GLY ALA GLY VAL LEU LEU LEU HIS          
SEQRES  29 E  617  PHE ASN VAL SER VAL LEU PRO VAL SER LEU HIS LEU PRO          
SEQRES  30 E  617  SER THR TYR SER LEU SER VAL SER ARG ARG ALA ARG ARG          
SEQRES  31 E  617  PHE ALA GLN ILE GLY LYS VAL CYS VAL GLU ASN CYS GLN          
SEQRES  32 E  617  ALA PHE SER GLY ILE ASN VAL GLN TYR LYS LEU HIS SER          
SEQRES  33 E  617  SER GLY ALA ASN CYS SER THR LEU GLY VAL VAL THR SER          
SEQRES  34 E  617  ALA GLU ASP THR SER GLY ILE LEU PHE VAL ASN ASP THR          
SEQRES  35 E  617  LYS ALA LEU ARG ARG PRO LYS CYS ALA GLU LEU HIS TYR          
SEQRES  36 E  617  MET VAL VAL ALA THR ASP GLN GLN THR SER ARG GLN ALA          
SEQRES  37 E  617  GLN ALA GLN LEU LEU VAL THR VAL GLU GLY SER TYR VAL          
SEQRES  38 E  617  ALA GLU GLU ALA GLY CYS PRO LEU SER CYS ALA VAL SER          
SEQRES  39 E  617  LYS ARG ARG LEU GLU CYS GLU GLU CYS GLY GLY LEU GLY          
SEQRES  40 E  617  SER PRO THR GLY ARG CYS GLU TRP ARG GLN GLY ASP GLY          
SEQRES  41 E  617  LYS GLY ILE THR ARG ASN PHE SER THR CYS SER PRO SER          
SEQRES  42 E  617  THR LYS THR CYS PRO ASP GLY HIS CYS ASP VAL VAL GLU          
SEQRES  43 E  617  THR GLN ASP ILE ASN ILE CYS PRO GLN ASP CYS LEU ARG          
SEQRES  44 E  617  GLY SER ILE VAL GLY GLY HIS GLU PRO GLY GLU PRO ARG          
SEQRES  45 E  617  GLY ILE LYS ALA GLY TYR GLY THR CYS ASN CYS PHE PRO          
SEQRES  46 E  617  GLU GLU GLU LYS CYS PHE CYS GLU PRO GLU ASP ILE GLN          
SEQRES  47 E  617  ASP PRO LEU CYS ASP GLU LEU CYS ARG GLY THR HIS HIS          
SEQRES  48 E  617  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 D  349  SER SER LEU GLN GLY PRO GLU LEU HIS GLY TRP ARG PRO          
SEQRES   2 D  349  PRO VAL ASP CYS VAL ARG ALA ASN GLU LEU CYS ALA ALA          
SEQRES   3 D  349  GLU SER ASN CYS SER SER ARG TYR ARG THR LEU ARG GLN          
SEQRES   4 D  349  CYS LEU ALA GLY ARG ASP ARG ASN THR MET LEU ALA ASN          
SEQRES   5 D  349  LYS GLU CYS GLN ALA ALA LEU GLU VAL LEU GLN GLU SER          
SEQRES   6 D  349  PRO LEU TYR ASP CYS ARG CYS LYS ARG GLY MET LYS LYS          
SEQRES   7 D  349  GLU LEU GLN CYS LEU GLN ILE TYR TRP SER ILE HIS LEU          
SEQRES   8 D  349  GLY LEU THR GLU GLY GLU GLU PHE TYR GLU ALA SER PRO          
SEQRES   9 D  349  TYR GLU PRO VAL THR SER ARG LEU SER ASP ILE PHE ARG          
SEQRES  10 D  349  LEU ALA SER ILE PHE SER GLY THR GLY ALA ASP PRO VAL          
SEQRES  11 D  349  VAL SER ALA LYS SER ASN HIS CYS LEU ASP ALA ALA LYS          
SEQRES  12 D  349  ALA CYS ASN LEU ASN ASP ASN CYS LYS LYS LEU ARG SER          
SEQRES  13 D  349  SER TYR ILE SER ILE CYS ASN ARG GLU ILE SER PRO THR          
SEQRES  14 D  349  GLU ARG CYS ASN ARG ARG LYS CYS HIS LYS ALA LEU ARG          
SEQRES  15 D  349  GLN PHE PHE ASP ARG VAL PRO SER GLU TYR THR TYR ARG          
SEQRES  16 D  349  MET LEU PHE CYS SER CYS GLN ASP GLN ALA CYS ALA GLU          
SEQRES  17 D  349  ARG ARG ARG GLN THR ILE LEU PRO SER CYS SER TYR GLU          
SEQRES  18 D  349  ASP LYS GLU LYS PRO ASN CYS LEU ASP LEU ARG GLY VAL          
SEQRES  19 D  349  CYS ARG THR ASP HIS LEU CYS ARG SER ARG LEU ALA ASP          
SEQRES  20 D  349  PHE HIS ALA ASN CYS ARG ALA SER TYR GLN THR VAL THR          
SEQRES  21 D  349  SER CYS PRO ALA ASP ASN TYR GLN ALA CYS LEU GLY SER          
SEQRES  22 D  349  TYR ALA GLY MET ILE GLY PHE ASP MET THR PRO ASN TYR          
SEQRES  23 D  349  VAL ASP SER SER PRO THR GLY ILE VAL VAL SER PRO TRP          
SEQRES  24 D  349  CYS SER CYS ARG GLY SER GLY ASN MET GLU GLU GLU CYS          
SEQRES  25 D  349  GLU LYS PHE LEU ARG ASP PHE THR GLU ASN PRO CYS LEU          
SEQRES  26 D  349  ARG ASN ALA ILE GLN ALA PHE GLY ASN GLY THR ASP VAL          
SEQRES  27 D  349  ASN GLY THR HIS HIS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 F  617  LEU TYR PHE SER ARG ASP ALA TYR TRP GLU LYS LEU TYR          
SEQRES   2 F  617  VAL ASP GLN ALA ALA GLY THR PRO LEU LEU TYR VAL HIS          
SEQRES   3 F  617  ALA LEU ARG ASP ALA PRO GLU GLU VAL PRO SER PHE ARG          
SEQRES   4 F  617  LEU GLY GLN HIS LEU TYR GLY THR TYR ARG THR ARG LEU          
SEQRES   5 F  617  HIS GLU ASN ASN TRP ILE CYS ILE GLN GLU ASP THR GLY          
SEQRES   6 F  617  LEU LEU TYR LEU ASN ARG SER LEU ASP HIS SER SER TRP          
SEQRES   7 F  617  GLU LYS LEU SER VAL ARG ASN HIS GLY PHE PRO LEU LEU          
SEQRES   8 F  617  THR VAL TYR LEU LYS VAL PHE LEU SER PRO THR SER LEU          
SEQRES   9 F  617  ARG GLU GLY GLU CYS GLN TRP PRO GLY CYS ALA ARG VAL          
SEQRES  10 F  617  TYR PHE SER PHE PHE ASN THR SER PHE PRO ALA CYS SER          
SEQRES  11 F  617  SER LEU LYS PRO ARG GLU LEU CYS PHE PRO GLU THR ARG          
SEQRES  12 F  617  PRO SER PHE ARG ILE ARG GLU ASN ARG PRO PRO GLY THR          
SEQRES  13 F  617  PHE HIS GLN PHE ARG LEU LEU PRO VAL GLN PHE LEU CYS          
SEQRES  14 F  617  PRO ASN ILE SER VAL ALA TYR ARG LEU LEU GLU GLY GLU          
SEQRES  15 F  617  GLY LEU PRO PHE ARG CYS ALA PRO ASP SER LEU GLU VAL          
SEQRES  16 F  617  SER THR ARG TRP ALA LEU ASP ARG GLU GLN ARG GLU LYS          
SEQRES  17 F  617  TYR GLU LEU VAL ALA VAL CYS THR VAL HIS ALA GLY ALA          
SEQRES  18 F  617  ARG GLU GLU VAL VAL MET VAL PRO PHE PRO VAL THR VAL          
SEQRES  19 F  617  TYR ASP GLU ASP ASP SER ALA PRO THR PHE PRO ALA GLY          
SEQRES  20 F  617  VAL ASP THR ALA SER ALA VAL VAL GLU PHE LYS ARG LYS          
SEQRES  21 F  617  GLU ASP THR VAL VAL ALA THR LEU ARG VAL PHE ASP ALA          
SEQRES  22 F  617  ASP VAL VAL PRO ALA SER GLY GLU LEU VAL ARG ARG TYR          
SEQRES  23 F  617  THR SER THR LEU LEU PRO GLY ASP THR TRP ALA GLN GLN          
SEQRES  24 F  617  THR PHE ARG VAL GLU HIS TRP PRO ASN GLU THR SER VAL          
SEQRES  25 F  617  GLN ALA ASN GLY SER PHE VAL ARG ALA THR VAL HIS ASP          
SEQRES  26 F  617  TYR ARG LEU VAL LEU ASN ARG ASN LEU SER ILE SER GLU          
SEQRES  27 F  617  ASN ARG THR MET GLN LEU ALA VAL LEU VAL ASN ASP SER          
SEQRES  28 F  617  ASP PHE GLN GLY PRO GLY ALA GLY VAL LEU LEU LEU HIS          
SEQRES  29 F  617  PHE ASN VAL SER VAL LEU PRO VAL SER LEU HIS LEU PRO          
SEQRES  30 F  617  SER THR TYR SER LEU SER VAL SER ARG ARG ALA ARG ARG          
SEQRES  31 F  617  PHE ALA GLN ILE GLY LYS VAL CYS VAL GLU ASN CYS GLN          
SEQRES  32 F  617  ALA PHE SER GLY ILE ASN VAL GLN TYR LYS LEU HIS SER          
SEQRES  33 F  617  SER GLY ALA ASN CYS SER THR LEU GLY VAL VAL THR SER          
SEQRES  34 F  617  ALA GLU ASP THR SER GLY ILE LEU PHE VAL ASN ASP THR          
SEQRES  35 F  617  LYS ALA LEU ARG ARG PRO LYS CYS ALA GLU LEU HIS TYR          
SEQRES  36 F  617  MET VAL VAL ALA THR ASP GLN GLN THR SER ARG GLN ALA          
SEQRES  37 F  617  GLN ALA GLN LEU LEU VAL THR VAL GLU GLY SER TYR VAL          
SEQRES  38 F  617  ALA GLU GLU ALA GLY CYS PRO LEU SER CYS ALA VAL SER          
SEQRES  39 F  617  LYS ARG ARG LEU GLU CYS GLU GLU CYS GLY GLY LEU GLY          
SEQRES  40 F  617  SER PRO THR GLY ARG CYS GLU TRP ARG GLN GLY ASP GLY          
SEQRES  41 F  617  LYS GLY ILE THR ARG ASN PHE SER THR CYS SER PRO SER          
SEQRES  42 F  617  THR LYS THR CYS PRO ASP GLY HIS CYS ASP VAL VAL GLU          
SEQRES  43 F  617  THR GLN ASP ILE ASN ILE CYS PRO GLN ASP CYS LEU ARG          
SEQRES  44 F  617  GLY SER ILE VAL GLY GLY HIS GLU PRO GLY GLU PRO ARG          
SEQRES  45 F  617  GLY ILE LYS ALA GLY TYR GLY THR CYS ASN CYS PHE PRO          
SEQRES  46 F  617  GLU GLU GLU LYS CYS PHE CYS GLU PRO GLU ASP ILE GLN          
SEQRES  47 F  617  ASP PRO LEU CYS ASP GLU LEU CYS ARG GLY THR HIS HIS          
SEQRES  48 F  617  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 U  102  ALA ARG LEU GLY ALA ARG PRO CYS GLY LEU ARG GLU LEU          
SEQRES   2 U  102  GLU VAL ARG VAL SER GLU LEU GLY LEU GLY TYR ALA SER          
SEQRES   3 U  102  ASP GLU THR VAL LEU PHE ARG TYR CYS ALA GLY ALA CYS          
SEQRES   4 U  102  GLU ALA ALA ALA ARG VAL TYR ASP LEU GLY LEU ARG ARG          
SEQRES   5 U  102  LEU ARG GLN ARG ARG ARG LEU ARG ARG GLU ARG VAL ARG          
SEQRES   6 U  102  ALA GLN PRO CYS CYS ARG PRO THR ALA TYR GLU ASP GLU          
SEQRES   7 U  102  VAL SER PHE LEU ASP ALA HIS SER ARG TYR HIS THR VAL          
SEQRES   8 U  102  HIS GLU LEU SER ALA ARG GLU CYS ALA CYS VAL                  
SEQRES   1 V  102  ALA ARG LEU GLY ALA ARG PRO CYS GLY LEU ARG GLU LEU          
SEQRES   2 V  102  GLU VAL ARG VAL SER GLU LEU GLY LEU GLY TYR ALA SER          
SEQRES   3 V  102  ASP GLU THR VAL LEU PHE ARG TYR CYS ALA GLY ALA CYS          
SEQRES   4 V  102  GLU ALA ALA ALA ARG VAL TYR ASP LEU GLY LEU ARG ARG          
SEQRES   5 V  102  LEU ARG GLN ARG ARG ARG LEU ARG ARG GLU ARG VAL ARG          
SEQRES   6 V  102  ALA GLN PRO CYS CYS ARG PRO THR ALA TYR GLU ASP GLU          
SEQRES   7 V  102  VAL SER PHE LEU ASP ALA HIS SER ARG TYR HIS THR VAL          
SEQRES   8 V  102  HIS GLU LEU SER ALA ARG GLU CYS ALA CYS VAL                  
SEQRES   1 W  349  SER SER LEU GLN GLY PRO GLU LEU HIS GLY TRP ARG PRO          
SEQRES   2 W  349  PRO VAL ASP CYS VAL ARG ALA ASN GLU LEU CYS ALA ALA          
SEQRES   3 W  349  GLU SER ASN CYS SER SER ARG TYR ARG THR LEU ARG GLN          
SEQRES   4 W  349  CYS LEU ALA GLY ARG ASP ARG ASN THR MET LEU ALA ASN          
SEQRES   5 W  349  LYS GLU CYS GLN ALA ALA LEU GLU VAL LEU GLN GLU SER          
SEQRES   6 W  349  PRO LEU TYR ASP CYS ARG CYS LYS ARG GLY MET LYS LYS          
SEQRES   7 W  349  GLU LEU GLN CYS LEU GLN ILE TYR TRP SER ILE HIS LEU          
SEQRES   8 W  349  GLY LEU THR GLU GLY GLU GLU PHE TYR GLU ALA SER PRO          
SEQRES   9 W  349  TYR GLU PRO VAL THR SER ARG LEU SER ASP ILE PHE ARG          
SEQRES  10 W  349  LEU ALA SER ILE PHE SER GLY THR GLY ALA ASP PRO VAL          
SEQRES  11 W  349  VAL SER ALA LYS SER ASN HIS CYS LEU ASP ALA ALA LYS          
SEQRES  12 W  349  ALA CYS ASN LEU ASN ASP ASN CYS LYS LYS LEU ARG SER          
SEQRES  13 W  349  SER TYR ILE SER ILE CYS ASN ARG GLU ILE SER PRO THR          
SEQRES  14 W  349  GLU ARG CYS ASN ARG ARG LYS CYS HIS LYS ALA LEU ARG          
SEQRES  15 W  349  GLN PHE PHE ASP ARG VAL PRO SER GLU TYR THR TYR ARG          
SEQRES  16 W  349  MET LEU PHE CYS SER CYS GLN ASP GLN ALA CYS ALA GLU          
SEQRES  17 W  349  ARG ARG ARG GLN THR ILE LEU PRO SER CYS SER TYR GLU          
SEQRES  18 W  349  ASP LYS GLU LYS PRO ASN CYS LEU ASP LEU ARG GLY VAL          
SEQRES  19 W  349  CYS ARG THR ASP HIS LEU CYS ARG SER ARG LEU ALA ASP          
SEQRES  20 W  349  PHE HIS ALA ASN CYS ARG ALA SER TYR GLN THR VAL THR          
SEQRES  21 W  349  SER CYS PRO ALA ASP ASN TYR GLN ALA CYS LEU GLY SER          
SEQRES  22 W  349  TYR ALA GLY MET ILE GLY PHE ASP MET THR PRO ASN TYR          
SEQRES  23 W  349  VAL ASP SER SER PRO THR GLY ILE VAL VAL SER PRO TRP          
SEQRES  24 W  349  CYS SER CYS ARG GLY SER GLY ASN MET GLU GLU GLU CYS          
SEQRES  25 W  349  GLU LYS PHE LEU ARG ASP PHE THR GLU ASN PRO CYS LEU          
SEQRES  26 W  349  ARG ASN ALA ILE GLN ALA PHE GLY ASN GLY THR ASP VAL          
SEQRES  27 W  349  ASN GLY THR HIS HIS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 Y  617  LEU TYR PHE SER ARG ASP ALA TYR TRP GLU LYS LEU TYR          
SEQRES   2 Y  617  VAL ASP GLN ALA ALA GLY THR PRO LEU LEU TYR VAL HIS          
SEQRES   3 Y  617  ALA LEU ARG ASP ALA PRO GLU GLU VAL PRO SER PHE ARG          
SEQRES   4 Y  617  LEU GLY GLN HIS LEU TYR GLY THR TYR ARG THR ARG LEU          
SEQRES   5 Y  617  HIS GLU ASN ASN TRP ILE CYS ILE GLN GLU ASP THR GLY          
SEQRES   6 Y  617  LEU LEU TYR LEU ASN ARG SER LEU ASP HIS SER SER TRP          
SEQRES   7 Y  617  GLU LYS LEU SER VAL ARG ASN HIS GLY PHE PRO LEU LEU          
SEQRES   8 Y  617  THR VAL TYR LEU LYS VAL PHE LEU SER PRO THR SER LEU          
SEQRES   9 Y  617  ARG GLU GLY GLU CYS GLN TRP PRO GLY CYS ALA ARG VAL          
SEQRES  10 Y  617  TYR PHE SER PHE PHE ASN THR SER PHE PRO ALA CYS SER          
SEQRES  11 Y  617  SER LEU LYS PRO ARG GLU LEU CYS PHE PRO GLU THR ARG          
SEQRES  12 Y  617  PRO SER PHE ARG ILE ARG GLU ASN ARG PRO PRO GLY THR          
SEQRES  13 Y  617  PHE HIS GLN PHE ARG LEU LEU PRO VAL GLN PHE LEU CYS          
SEQRES  14 Y  617  PRO ASN ILE SER VAL ALA TYR ARG LEU LEU GLU GLY GLU          
SEQRES  15 Y  617  GLY LEU PRO PHE ARG CYS ALA PRO ASP SER LEU GLU VAL          
SEQRES  16 Y  617  SER THR ARG TRP ALA LEU ASP ARG GLU GLN ARG GLU LYS          
SEQRES  17 Y  617  TYR GLU LEU VAL ALA VAL CYS THR VAL HIS ALA GLY ALA          
SEQRES  18 Y  617  ARG GLU GLU VAL VAL MET VAL PRO PHE PRO VAL THR VAL          
SEQRES  19 Y  617  TYR ASP GLU ASP ASP SER ALA PRO THR PHE PRO ALA GLY          
SEQRES  20 Y  617  VAL ASP THR ALA SER ALA VAL VAL GLU PHE LYS ARG LYS          
SEQRES  21 Y  617  GLU ASP THR VAL VAL ALA THR LEU ARG VAL PHE ASP ALA          
SEQRES  22 Y  617  ASP VAL VAL PRO ALA SER GLY GLU LEU VAL ARG ARG TYR          
SEQRES  23 Y  617  THR SER THR LEU LEU PRO GLY ASP THR TRP ALA GLN GLN          
SEQRES  24 Y  617  THR PHE ARG VAL GLU HIS TRP PRO ASN GLU THR SER VAL          
SEQRES  25 Y  617  GLN ALA ASN GLY SER PHE VAL ARG ALA THR VAL HIS ASP          
SEQRES  26 Y  617  TYR ARG LEU VAL LEU ASN ARG ASN LEU SER ILE SER GLU          
SEQRES  27 Y  617  ASN ARG THR MET GLN LEU ALA VAL LEU VAL ASN ASP SER          
SEQRES  28 Y  617  ASP PHE GLN GLY PRO GLY ALA GLY VAL LEU LEU LEU HIS          
SEQRES  29 Y  617  PHE ASN VAL SER VAL LEU PRO VAL SER LEU HIS LEU PRO          
SEQRES  30 Y  617  SER THR TYR SER LEU SER VAL SER ARG ARG ALA ARG ARG          
SEQRES  31 Y  617  PHE ALA GLN ILE GLY LYS VAL CYS VAL GLU ASN CYS GLN          
SEQRES  32 Y  617  ALA PHE SER GLY ILE ASN VAL GLN TYR LYS LEU HIS SER          
SEQRES  33 Y  617  SER GLY ALA ASN CYS SER THR LEU GLY VAL VAL THR SER          
SEQRES  34 Y  617  ALA GLU ASP THR SER GLY ILE LEU PHE VAL ASN ASP THR          
SEQRES  35 Y  617  LYS ALA LEU ARG ARG PRO LYS CYS ALA GLU LEU HIS TYR          
SEQRES  36 Y  617  MET VAL VAL ALA THR ASP GLN GLN THR SER ARG GLN ALA          
SEQRES  37 Y  617  GLN ALA GLN LEU LEU VAL THR VAL GLU GLY SER TYR VAL          
SEQRES  38 Y  617  ALA GLU GLU ALA GLY CYS PRO LEU SER CYS ALA VAL SER          
SEQRES  39 Y  617  LYS ARG ARG LEU GLU CYS GLU GLU CYS GLY GLY LEU GLY          
SEQRES  40 Y  617  SER PRO THR GLY ARG CYS GLU TRP ARG GLN GLY ASP GLY          
SEQRES  41 Y  617  LYS GLY ILE THR ARG ASN PHE SER THR CYS SER PRO SER          
SEQRES  42 Y  617  THR LYS THR CYS PRO ASP GLY HIS CYS ASP VAL VAL GLU          
SEQRES  43 Y  617  THR GLN ASP ILE ASN ILE CYS PRO GLN ASP CYS LEU ARG          
SEQRES  44 Y  617  GLY SER ILE VAL GLY GLY HIS GLU PRO GLY GLU PRO ARG          
SEQRES  45 Y  617  GLY ILE LYS ALA GLY TYR GLY THR CYS ASN CYS PHE PRO          
SEQRES  46 Y  617  GLU GLU GLU LYS CYS PHE CYS GLU PRO GLU ASP ILE GLN          
SEQRES  47 Y  617  ASP PRO LEU CYS ASP GLU LEU CYS ARG GLY THR HIS HIS          
SEQRES  48 Y  617  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 X  349  SER SER LEU GLN GLY PRO GLU LEU HIS GLY TRP ARG PRO          
SEQRES   2 X  349  PRO VAL ASP CYS VAL ARG ALA ASN GLU LEU CYS ALA ALA          
SEQRES   3 X  349  GLU SER ASN CYS SER SER ARG TYR ARG THR LEU ARG GLN          
SEQRES   4 X  349  CYS LEU ALA GLY ARG ASP ARG ASN THR MET LEU ALA ASN          
SEQRES   5 X  349  LYS GLU CYS GLN ALA ALA LEU GLU VAL LEU GLN GLU SER          
SEQRES   6 X  349  PRO LEU TYR ASP CYS ARG CYS LYS ARG GLY MET LYS LYS          
SEQRES   7 X  349  GLU LEU GLN CYS LEU GLN ILE TYR TRP SER ILE HIS LEU          
SEQRES   8 X  349  GLY LEU THR GLU GLY GLU GLU PHE TYR GLU ALA SER PRO          
SEQRES   9 X  349  TYR GLU PRO VAL THR SER ARG LEU SER ASP ILE PHE ARG          
SEQRES  10 X  349  LEU ALA SER ILE PHE SER GLY THR GLY ALA ASP PRO VAL          
SEQRES  11 X  349  VAL SER ALA LYS SER ASN HIS CYS LEU ASP ALA ALA LYS          
SEQRES  12 X  349  ALA CYS ASN LEU ASN ASP ASN CYS LYS LYS LEU ARG SER          
SEQRES  13 X  349  SER TYR ILE SER ILE CYS ASN ARG GLU ILE SER PRO THR          
SEQRES  14 X  349  GLU ARG CYS ASN ARG ARG LYS CYS HIS LYS ALA LEU ARG          
SEQRES  15 X  349  GLN PHE PHE ASP ARG VAL PRO SER GLU TYR THR TYR ARG          
SEQRES  16 X  349  MET LEU PHE CYS SER CYS GLN ASP GLN ALA CYS ALA GLU          
SEQRES  17 X  349  ARG ARG ARG GLN THR ILE LEU PRO SER CYS SER TYR GLU          
SEQRES  18 X  349  ASP LYS GLU LYS PRO ASN CYS LEU ASP LEU ARG GLY VAL          
SEQRES  19 X  349  CYS ARG THR ASP HIS LEU CYS ARG SER ARG LEU ALA ASP          
SEQRES  20 X  349  PHE HIS ALA ASN CYS ARG ALA SER TYR GLN THR VAL THR          
SEQRES  21 X  349  SER CYS PRO ALA ASP ASN TYR GLN ALA CYS LEU GLY SER          
SEQRES  22 X  349  TYR ALA GLY MET ILE GLY PHE ASP MET THR PRO ASN TYR          
SEQRES  23 X  349  VAL ASP SER SER PRO THR GLY ILE VAL VAL SER PRO TRP          
SEQRES  24 X  349  CYS SER CYS ARG GLY SER GLY ASN MET GLU GLU GLU CYS          
SEQRES  25 X  349  GLU LYS PHE LEU ARG ASP PHE THR GLU ASN PRO CYS LEU          
SEQRES  26 X  349  ARG ASN ALA ILE GLN ALA PHE GLY ASN GLY THR ASP VAL          
SEQRES  27 X  349  ASN GLY THR HIS HIS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 Z  617  LEU TYR PHE SER ARG ASP ALA TYR TRP GLU LYS LEU TYR          
SEQRES   2 Z  617  VAL ASP GLN ALA ALA GLY THR PRO LEU LEU TYR VAL HIS          
SEQRES   3 Z  617  ALA LEU ARG ASP ALA PRO GLU GLU VAL PRO SER PHE ARG          
SEQRES   4 Z  617  LEU GLY GLN HIS LEU TYR GLY THR TYR ARG THR ARG LEU          
SEQRES   5 Z  617  HIS GLU ASN ASN TRP ILE CYS ILE GLN GLU ASP THR GLY          
SEQRES   6 Z  617  LEU LEU TYR LEU ASN ARG SER LEU ASP HIS SER SER TRP          
SEQRES   7 Z  617  GLU LYS LEU SER VAL ARG ASN HIS GLY PHE PRO LEU LEU          
SEQRES   8 Z  617  THR VAL TYR LEU LYS VAL PHE LEU SER PRO THR SER LEU          
SEQRES   9 Z  617  ARG GLU GLY GLU CYS GLN TRP PRO GLY CYS ALA ARG VAL          
SEQRES  10 Z  617  TYR PHE SER PHE PHE ASN THR SER PHE PRO ALA CYS SER          
SEQRES  11 Z  617  SER LEU LYS PRO ARG GLU LEU CYS PHE PRO GLU THR ARG          
SEQRES  12 Z  617  PRO SER PHE ARG ILE ARG GLU ASN ARG PRO PRO GLY THR          
SEQRES  13 Z  617  PHE HIS GLN PHE ARG LEU LEU PRO VAL GLN PHE LEU CYS          
SEQRES  14 Z  617  PRO ASN ILE SER VAL ALA TYR ARG LEU LEU GLU GLY GLU          
SEQRES  15 Z  617  GLY LEU PRO PHE ARG CYS ALA PRO ASP SER LEU GLU VAL          
SEQRES  16 Z  617  SER THR ARG TRP ALA LEU ASP ARG GLU GLN ARG GLU LYS          
SEQRES  17 Z  617  TYR GLU LEU VAL ALA VAL CYS THR VAL HIS ALA GLY ALA          
SEQRES  18 Z  617  ARG GLU GLU VAL VAL MET VAL PRO PHE PRO VAL THR VAL          
SEQRES  19 Z  617  TYR ASP GLU ASP ASP SER ALA PRO THR PHE PRO ALA GLY          
SEQRES  20 Z  617  VAL ASP THR ALA SER ALA VAL VAL GLU PHE LYS ARG LYS          
SEQRES  21 Z  617  GLU ASP THR VAL VAL ALA THR LEU ARG VAL PHE ASP ALA          
SEQRES  22 Z  617  ASP VAL VAL PRO ALA SER GLY GLU LEU VAL ARG ARG TYR          
SEQRES  23 Z  617  THR SER THR LEU LEU PRO GLY ASP THR TRP ALA GLN GLN          
SEQRES  24 Z  617  THR PHE ARG VAL GLU HIS TRP PRO ASN GLU THR SER VAL          
SEQRES  25 Z  617  GLN ALA ASN GLY SER PHE VAL ARG ALA THR VAL HIS ASP          
SEQRES  26 Z  617  TYR ARG LEU VAL LEU ASN ARG ASN LEU SER ILE SER GLU          
SEQRES  27 Z  617  ASN ARG THR MET GLN LEU ALA VAL LEU VAL ASN ASP SER          
SEQRES  28 Z  617  ASP PHE GLN GLY PRO GLY ALA GLY VAL LEU LEU LEU HIS          
SEQRES  29 Z  617  PHE ASN VAL SER VAL LEU PRO VAL SER LEU HIS LEU PRO          
SEQRES  30 Z  617  SER THR TYR SER LEU SER VAL SER ARG ARG ALA ARG ARG          
SEQRES  31 Z  617  PHE ALA GLN ILE GLY LYS VAL CYS VAL GLU ASN CYS GLN          
SEQRES  32 Z  617  ALA PHE SER GLY ILE ASN VAL GLN TYR LYS LEU HIS SER          
SEQRES  33 Z  617  SER GLY ALA ASN CYS SER THR LEU GLY VAL VAL THR SER          
SEQRES  34 Z  617  ALA GLU ASP THR SER GLY ILE LEU PHE VAL ASN ASP THR          
SEQRES  35 Z  617  LYS ALA LEU ARG ARG PRO LYS CYS ALA GLU LEU HIS TYR          
SEQRES  36 Z  617  MET VAL VAL ALA THR ASP GLN GLN THR SER ARG GLN ALA          
SEQRES  37 Z  617  GLN ALA GLN LEU LEU VAL THR VAL GLU GLY SER TYR VAL          
SEQRES  38 Z  617  ALA GLU GLU ALA GLY CYS PRO LEU SER CYS ALA VAL SER          
SEQRES  39 Z  617  LYS ARG ARG LEU GLU CYS GLU GLU CYS GLY GLY LEU GLY          
SEQRES  40 Z  617  SER PRO THR GLY ARG CYS GLU TRP ARG GLN GLY ASP GLY          
SEQRES  41 Z  617  LYS GLY ILE THR ARG ASN PHE SER THR CYS SER PRO SER          
SEQRES  42 Z  617  THR LYS THR CYS PRO ASP GLY HIS CYS ASP VAL VAL GLU          
SEQRES  43 Z  617  THR GLN ASP ILE ASN ILE CYS PRO GLN ASP CYS LEU ARG          
SEQRES  44 Z  617  GLY SER ILE VAL GLY GLY HIS GLU PRO GLY GLU PRO ARG          
SEQRES  45 Z  617  GLY ILE LYS ALA GLY TYR GLY THR CYS ASN CYS PHE PRO          
SEQRES  46 Z  617  GLU GLU GLU LYS CYS PHE CYS GLU PRO GLU ASP ILE GLN          
SEQRES  47 Z  617  ASP PRO LEU CYS ASP GLU LEU CYS ARG GLY THR HIS HIS          
SEQRES  48 Z  617  HIS HIS HIS HIS HIS HIS                                      
HET     CA  E2001       1                                                       
HET     CA  E2002       1                                                       
HET     CA  E2003       1                                                       
HET     CA  E2004       1                                                       
HET    NAG  E2005      14                                                       
HET    NAG  E2006      14                                                       
HET    NAG  E2007      14                                                       
HET    NAG  E2008      14                                                       
HET    NAG  E2009      14                                                       
HET    NAG  E2010      14                                                       
HET     CA  F2001       1                                                       
HET     CA  F2002       1                                                       
HET     CA  F2003       1                                                       
HET     CA  F2004       1                                                       
HET    NAG  F2005      14                                                       
HET    NAG  F2006      14                                                       
HET    NAG  F2007      14                                                       
HET    NAG  F2008      14                                                       
HET    NAG  F2009      14                                                       
HET    NAG  F2010      14                                                       
HET     CA  Y2001       1                                                       
HET     CA  Y2002       1                                                       
HET     CA  Y2003       1                                                       
HET     CA  Y2004       1                                                       
HET    NAG  Y2005      14                                                       
HET    NAG  Y2006      14                                                       
HET    NAG  Y2007      14                                                       
HET    NAG  Y2008      14                                                       
HET    NAG  Y2009      14                                                       
HET    NAG  Y2010      14                                                       
HET     CA  Z2001       1                                                       
HET     CA  Z2002       1                                                       
HET     CA  Z2003       1                                                       
HET     CA  Z2004       1                                                       
HET    NAG  Z2005      14                                                       
HET    NAG  Z2006      14                                                       
HET    NAG  Z2007      14                                                       
HET    NAG  Z2008      14                                                       
HET    NAG  Z2009      14                                                       
HET    NAG  Z2010      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL  13   CA    16(CA 2+)                                                    
FORMUL  17  NAG    24(C8 H15 N O6)                                              
HELIX    1 AA1 SER A  113  GLY A  116  5                                   4    
HELIX    2 AA2 ARG A  139  ARG A  152  1                                  14    
HELIX    3 AA3 SER B  113  GLY B  116  5                                   4    
HELIX    4 AA4 ARG B  139  ARG B  151  1                                  13    
HELIX    5 AA5 ASP C   39  ALA C   49  1                                  11    
HELIX    6 AA6 SER C   51  ALA C   65  1                                  15    
HELIX    7 AA7 LYS C   76  GLN C   86  1                                  11    
HELIX    8 AA8 LYS C  101  ILE C  112  1                                  12    
HELIX    9 AA9 HIS C  160  LEU C  170  1                                  11    
HELIX   10 AB1 ASN C  171  ASN C  186  1                                  16    
HELIX   11 AB2 ASN C  196  PHE C  208  1                                  13    
HELIX   12 AB3 PRO C  212  PHE C  221  1                                  10    
HELIX   13 AB4 ASP C  226  GLN C  235  1                                  10    
HELIX   14 AB5 THR C  236  LEU C  238  5                                   3    
HELIX   15 AB6 ASN C  250  ASP C  261  1                                  12    
HELIX   16 AB7 ASP C  261  CYS C  275  1                                  15    
HELIX   17 AB8 CYS C  285  ASP C  288  5                                   4    
HELIX   18 AB9 ASN C  289  GLY C  299  1                                  11    
HELIX   19 AC1 MET C  331  GLU C  344  1                                  14    
HELIX   20 AC2 ASN C  345  ASN C  357  1                                  13    
HELIX   21 AC3 ASP E  102  SER E  110  1                                   9    
HELIX   22 AC4 VAL E  111  HIS E  114  5                                   4    
HELIX   23 AC5 PRO E  162  PHE E  167  1                                   6    
HELIX   24 AC6 LEU E  190  CYS E  197  1                                   8    
HELIX   25 AC7 GLU E  309  ARG E  313  1                                   5    
HELIX   26 AC8 ASP E  322  THR E  328  1                                   7    
HELIX   27 AC9 ASN E  429  PHE E  433  5                                   5    
HELIX   28 AD1 THR E  470  ARG E  475  1                                   6    
HELIX   29 AD2 SER E  518  SER E  522  5                                   5    
HELIX   30 AD3 ARG E  525  GLU E  530  1                                   6    
HELIX   31 AD4 THR E  564  GLY E  568  5                                   5    
HELIX   32 AD5 CYS E  581  LEU E  586  1                                   6    
HELIX   33 AD6 ASP D   39  ALA D   49  1                                  11    
HELIX   34 AD7 SER D   51  ALA D   65  1                                  15    
HELIX   35 AD8 LYS D   76  GLN D   86  1                                  11    
HELIX   36 AD9 LYS D  101  ILE D  112  1                                  12    
HELIX   37 AE1 HIS D  160  LEU D  170  1                                  11    
HELIX   38 AE2 ASN D  171  ASN D  186  1                                  16    
HELIX   39 AE3 ASN D  196  PHE D  208  1                                  13    
HELIX   40 AE4 PRO D  212  PHE D  221  1                                  10    
HELIX   41 AE5 ASP D  226  GLN D  235  1                                  10    
HELIX   42 AE6 THR D  236  LEU D  238  5                                   3    
HELIX   43 AE7 ASN D  250  ASP D  261  1                                  12    
HELIX   44 AE8 ASP D  261  CYS D  275  1                                  15    
HELIX   45 AE9 CYS D  285  ASP D  288  5                                   4    
HELIX   46 AF1 ASN D  289  GLY D  299  1                                  11    
HELIX   47 AF2 MET D  331  GLU D  344  1                                  14    
HELIX   48 AF3 ASN D  345  ASN D  357  1                                  13    
HELIX   49 AF4 ASP F  102  SER F  110  1                                   9    
HELIX   50 AF5 VAL F  111  HIS F  114  5                                   4    
HELIX   51 AF6 PRO F  162  PHE F  167  1                                   6    
HELIX   52 AF7 LEU F  190  CYS F  197  1                                   8    
HELIX   53 AF8 GLU F  309  ARG F  313  1                                   5    
HELIX   54 AF9 ASP F  322  THR F  328  1                                   7    
HELIX   55 AG1 ASN F  429  PHE F  433  5                                   5    
HELIX   56 AG2 THR F  470  ARG F  475  1                                   6    
HELIX   57 AG3 SER F  518  SER F  522  5                                   5    
HELIX   58 AG4 ARG F  525  GLU F  530  1                                   6    
HELIX   59 AG5 THR F  564  GLY F  568  5                                   5    
HELIX   60 AG6 CYS F  581  LEU F  586  1                                   6    
HELIX   61 AG7 SER U  113  GLY U  116  5                                   4    
HELIX   62 AG8 ARG U  139  ARG U  152  1                                  14    
HELIX   63 AG9 SER V  113  GLY V  116  5                                   4    
HELIX   64 AH1 ARG V  139  ARG V  151  1                                  13    
HELIX   65 AH2 ASP W   39  ALA W   49  1                                  11    
HELIX   66 AH3 SER W   51  ALA W   65  1                                  15    
HELIX   67 AH4 LYS W   76  GLN W   86  1                                  11    
HELIX   68 AH5 LYS W  101  ILE W  112  1                                  12    
HELIX   69 AH6 HIS W  160  LEU W  170  1                                  11    
HELIX   70 AH7 ASN W  171  ASN W  186  1                                  16    
HELIX   71 AH8 ASN W  196  PHE W  208  1                                  13    
HELIX   72 AH9 PRO W  212  PHE W  221  1                                  10    
HELIX   73 AI1 ASP W  226  GLN W  235  1                                  10    
HELIX   74 AI2 THR W  236  LEU W  238  5                                   3    
HELIX   75 AI3 ASN W  250  ASP W  261  1                                  12    
HELIX   76 AI4 ASP W  261  CYS W  275  1                                  15    
HELIX   77 AI5 CYS W  285  ASP W  288  5                                   4    
HELIX   78 AI6 ASN W  289  GLY W  299  1                                  11    
HELIX   79 AI7 MET W  331  GLU W  344  1                                  14    
HELIX   80 AI8 ASN W  345  ASN W  357  1                                  13    
HELIX   81 AI9 ASP Y  102  SER Y  110  1                                   9    
HELIX   82 AJ1 VAL Y  111  HIS Y  114  5                                   4    
HELIX   83 AJ2 PRO Y  162  PHE Y  167  1                                   6    
HELIX   84 AJ3 LEU Y  190  CYS Y  197  1                                   8    
HELIX   85 AJ4 GLU Y  309  ARG Y  313  1                                   5    
HELIX   86 AJ5 ASP Y  322  THR Y  328  1                                   7    
HELIX   87 AJ6 ASN Y  429  PHE Y  433  5                                   5    
HELIX   88 AJ7 THR Y  470  ARG Y  475  1                                   6    
HELIX   89 AJ8 SER Y  518  SER Y  522  5                                   5    
HELIX   90 AJ9 ARG Y  525  GLU Y  530  1                                   6    
HELIX   91 AK1 THR Y  564  GLY Y  568  5                                   5    
HELIX   92 AK2 CYS Y  581  LEU Y  586  1                                   6    
HELIX   93 AK3 ASP X   39  ALA X   49  1                                  11    
HELIX   94 AK4 SER X   51  ALA X   65  1                                  15    
HELIX   95 AK5 LYS X   76  GLN X   86  1                                  11    
HELIX   96 AK6 LYS X  101  ILE X  112  1                                  12    
HELIX   97 AK7 HIS X  160  LEU X  170  1                                  11    
HELIX   98 AK8 ASN X  171  ASN X  186  1                                  16    
HELIX   99 AK9 ASN X  196  PHE X  208  1                                  13    
HELIX  100 AL1 PRO X  212  PHE X  221  1                                  10    
HELIX  101 AL2 ASP X  226  GLN X  235  1                                  10    
HELIX  102 AL3 THR X  236  LEU X  238  5                                   3    
HELIX  103 AL4 ASN X  250  ASP X  261  1                                  12    
HELIX  104 AL5 ASP X  261  CYS X  275  1                                  15    
HELIX  105 AL6 CYS X  285  ASP X  288  5                                   4    
HELIX  106 AL7 ASN X  289  GLY X  299  1                                  11    
HELIX  107 AL8 MET X  331  GLU X  344  1                                  14    
HELIX  108 AL9 ASN X  345  ASN X  357  1                                  13    
HELIX  109 AM1 ASP Z  102  SER Z  110  1                                   9    
HELIX  110 AM2 VAL Z  111  HIS Z  114  5                                   4    
HELIX  111 AM3 PRO Z  162  PHE Z  167  1                                   6    
HELIX  112 AM4 LEU Z  190  CYS Z  197  1                                   8    
HELIX  113 AM5 GLU Z  309  ARG Z  313  1                                   5    
HELIX  114 AM6 ASP Z  322  THR Z  328  1                                   7    
HELIX  115 AM7 ASN Z  429  PHE Z  433  5                                   5    
HELIX  116 AM8 THR Z  470  ARG Z  475  1                                   6    
HELIX  117 AM9 SER Z  518  SER Z  522  5                                   5    
HELIX  118 AN1 ARG Z  525  GLU Z  530  1                                   6    
HELIX  119 AN2 THR Z  564  GLY Z  568  5                                   5    
HELIX  120 AN3 CYS Z  581  LEU Z  586  1                                   6    
SHEET    1 AA1 2 GLY A 104  ARG A 111  0                                        
SHEET    2 AA1 2 THR A 124  ALA A 131 -1  O  VAL A 125   N  VAL A 110           
SHEET    1 AA2 2 CYS A 165  PRO A 167  0                                        
SHEET    2 AA2 2 CYS A 194  CYS A 196 -1  O  ALA A 195   N  ARG A 166           
SHEET    1 AA3 2 GLU A 173  LEU A 177  0                                        
SHEET    2 AA3 2 TYR A 183  HIS A 187 -1  O  VAL A 186   N  VAL A 174           
SHEET    1 AA4 2 GLY B 104  ARG B 111  0                                        
SHEET    2 AA4 2 THR B 124  ALA B 131 -1  O  VAL B 125   N  VAL B 110           
SHEET    1 AA5 2 CYS B 165  PRO B 167  0                                        
SHEET    2 AA5 2 CYS B 194  CYS B 196 -1  O  ALA B 195   N  ARG B 166           
SHEET    1 AA6 2 GLU B 173  LEU B 177  0                                        
SHEET    2 AA6 2 TYR B 183  HIS B 187 -1  O  HIS B 184   N  PHE B 176           
SHEET    1 AA7 2 ASN C 308  TYR C 309  0                                        
SHEET    2 AA7 2 VAL C 319  SER C 320 -1  O  SER C 320   N  ASN C 308           
SHEET    1 AA8 2 TYR E  30  PHE E  31  0                                        
SHEET    2 AA8 2 ALA E  55  LEU E  56 -1  O  LEU E  56   N  TYR E  30           
SHEET    1 AA9 3 ALA E  35  TYR E  36  0                                        
SHEET    2 AA9 3 ALA E 143  PHE E 149  1  O  TYR E 146   N  TYR E  36           
SHEET    3 AA9 3 LYS E  39  LEU E  40  1  N  LEU E  40   O  SER E 148           
SHEET    1 AB1 4 ALA E  35  TYR E  36  0                                        
SHEET    2 AB1 4 ALA E 143  PHE E 149  1  O  TYR E 146   N  TYR E  36           
SHEET    3 AB1 4 THR E 120  PHE E 126 -1  N  VAL E 121   O  PHE E 147           
SHEET    4 AB1 4 ARG E  67  LEU E  68 -1  N  ARG E  67   O  PHE E 126           
SHEET    1 AB2 3 PRO E  49  TYR E  52  0                                        
SHEET    2 AB2 3 LEU E  94  LEU E  97 -1  O  LEU E  95   N  LEU E  50           
SHEET    3 AB2 3 ILE E  86  GLN E  89 -1  N  CYS E  87   O  TYR E  96           
SHEET    1 AB3 2 LEU E  72  TYR E  73  0                                        
SHEET    2 AB3 2 ARG E  79  HIS E  81 -1  O  HIS E  81   N  LEU E  72           
SHEET    1 AB4 4 PHE E 174  ILE E 176  0                                        
SHEET    2 AB4 4 GLU E 252  VAL E 262  1  O  THR E 261   N  ILE E 176           
SHEET    3 AB4 4 LYS E 236  VAL E 245 -1  N  ALA E 241   O  VAL E 256           
SHEET    4 AB4 4 VAL E 202  ARG E 205 -1  N  ARG E 205   O  VAL E 242           
SHEET    1 AB5 3 THR E 184  GLN E 187  0                                        
SHEET    2 AB5 3 GLU E 222  THR E 225 -1  O  VAL E 223   N  HIS E 186           
SHEET    3 AB5 3 PHE E 214  CYS E 216 -1  N  ARG E 215   O  SER E 224           
SHEET    1 AB6 4 SER E 280  VAL E 283  0                                        
SHEET    2 AB6 4 VAL E 388  VAL E 397  1  O  ASN E 394   N  ALA E 281           
SHEET    3 AB6 4 ARG E 368  ASP E 378 -1  N  MET E 370   O  VAL E 395           
SHEET    4 AB6 4 TYR E 314  LEU E 318 -1  N  THR E 317   O  LEU E 375           
SHEET    1 AB7 3 VAL E 292  ASP E 300  0                                        
SHEET    2 AB7 3 VAL E 347  LEU E 358 -1  O  LEU E 356   N  VAL E 293           
SHEET    3 AB7 3 PHE E 329  VAL E 340 -1  N  GLU E 332   O  ARG E 355           
SHEET    1 AB8 4 LEU E 410  SER E 413  0                                        
SHEET    2 AB8 4 ALA E 496  GLU E 505  1  O  GLU E 505   N  VAL E 412           
SHEET    3 AB8 4 GLU E 480  ALA E 487 -1  N  TYR E 483   O  LEU E 500           
SHEET    4 AB8 4 TYR E 440  LYS E 441 -1  N  LYS E 441   O  VAL E 486           
SHEET    1 AB9 3 GLN E 421  VAL E 425  0                                        
SHEET    2 AB9 3 SER E 462  VAL E 467 -1  O  LEU E 465   N  GLY E 423           
SHEET    3 AB9 3 LEU E 452  SER E 457 -1  N  SER E 457   O  SER E 462           
SHEET    1 AC1 2 GLU E 542  ARG E 544  0                                        
SHEET    2 AC1 2 THR E 557  SER E 559 -1  O  SER E 559   N  GLU E 542           
SHEET    1 AC2 3 SER E 589  VAL E 591  0                                        
SHEET    2 AC2 3 LYS E 617  GLU E 621  1  O  CYS E 618   N  VAL E 591           
SHEET    3 AC2 3 THR E 608  PHE E 612 -1  N  ASN E 610   O  PHE E 619           
SHEET    1 AC3 2 GLU E 595  PRO E 596  0                                        
SHEET    2 AC3 2 ILE E 602  ALA E 604 -1  O  ALA E 604   N  GLU E 595           
SHEET    1 AC4 2 ASN D 308  TYR D 309  0                                        
SHEET    2 AC4 2 VAL D 319  SER D 320 -1  O  SER D 320   N  ASN D 308           
SHEET    1 AC5 2 TYR F  30  PHE F  31  0                                        
SHEET    2 AC5 2 ALA F  55  LEU F  56 -1  O  LEU F  56   N  TYR F  30           
SHEET    1 AC6 3 ALA F  35  TYR F  36  0                                        
SHEET    2 AC6 3 ALA F 143  PHE F 149  1  O  TYR F 146   N  TYR F  36           
SHEET    3 AC6 3 LYS F  39  LEU F  40  1  N  LEU F  40   O  SER F 148           
SHEET    1 AC7 4 ALA F  35  TYR F  36  0                                        
SHEET    2 AC7 4 ALA F 143  PHE F 149  1  O  TYR F 146   N  TYR F  36           
SHEET    3 AC7 4 THR F 120  PHE F 126 -1  N  VAL F 121   O  PHE F 147           
SHEET    4 AC7 4 ARG F  67  LEU F  68 -1  N  ARG F  67   O  PHE F 126           
SHEET    1 AC8 3 PRO F  49  TYR F  52  0                                        
SHEET    2 AC8 3 LEU F  94  LEU F  97 -1  O  LEU F  95   N  LEU F  50           
SHEET    3 AC8 3 ILE F  86  GLN F  89 -1  N  CYS F  87   O  TYR F  96           
SHEET    1 AC9 2 LEU F  72  TYR F  73  0                                        
SHEET    2 AC9 2 ARG F  79  HIS F  81 -1  O  HIS F  81   N  LEU F  72           
SHEET    1 AD1 4 PHE F 174  ILE F 176  0                                        
SHEET    2 AD1 4 GLU F 252  VAL F 262  1  O  THR F 261   N  ILE F 176           
SHEET    3 AD1 4 LYS F 236  VAL F 245 -1  N  ALA F 241   O  VAL F 256           
SHEET    4 AD1 4 VAL F 202  ARG F 205 -1  N  ARG F 205   O  VAL F 242           
SHEET    1 AD2 3 THR F 184  GLN F 187  0                                        
SHEET    2 AD2 3 GLU F 222  THR F 225 -1  O  VAL F 223   N  HIS F 186           
SHEET    3 AD2 3 PHE F 214  CYS F 216 -1  N  ARG F 215   O  SER F 224           
SHEET    1 AD3 4 SER F 280  VAL F 283  0                                        
SHEET    2 AD3 4 VAL F 388  VAL F 397  1  O  ASN F 394   N  ALA F 281           
SHEET    3 AD3 4 ARG F 368  ASP F 378 -1  N  MET F 370   O  VAL F 395           
SHEET    4 AD3 4 TYR F 314  LEU F 318 -1  N  THR F 317   O  LEU F 375           
SHEET    1 AD4 3 VAL F 292  ASP F 300  0                                        
SHEET    2 AD4 3 VAL F 347  LEU F 358 -1  O  LEU F 356   N  VAL F 293           
SHEET    3 AD4 3 PHE F 329  VAL F 340 -1  N  GLU F 332   O  ARG F 355           
SHEET    1 AD5 4 LEU F 410  SER F 413  0                                        
SHEET    2 AD5 4 ALA F 496  GLU F 505  1  O  GLU F 505   N  VAL F 412           
SHEET    3 AD5 4 GLU F 480  ALA F 487 -1  N  TYR F 483   O  LEU F 500           
SHEET    4 AD5 4 TYR F 440  LYS F 441 -1  N  LYS F 441   O  VAL F 486           
SHEET    1 AD6 3 GLN F 421  VAL F 425  0                                        
SHEET    2 AD6 3 SER F 462  VAL F 467 -1  O  LEU F 465   N  GLY F 423           
SHEET    3 AD6 3 LEU F 452  SER F 457 -1  N  SER F 457   O  SER F 462           
SHEET    1 AD7 2 GLU F 542  ARG F 544  0                                        
SHEET    2 AD7 2 THR F 557  SER F 559 -1  O  SER F 559   N  GLU F 542           
SHEET    1 AD8 3 SER F 589  VAL F 591  0                                        
SHEET    2 AD8 3 LYS F 617  GLU F 621  1  O  CYS F 618   N  VAL F 591           
SHEET    3 AD8 3 THR F 608  PHE F 612 -1  N  ASN F 610   O  PHE F 619           
SHEET    1 AD9 2 GLU F 595  PRO F 596  0                                        
SHEET    2 AD9 2 ILE F 602  ALA F 604 -1  O  ALA F 604   N  GLU F 595           
SHEET    1 AE1 2 GLY U 104  ARG U 111  0                                        
SHEET    2 AE1 2 THR U 124  ALA U 131 -1  O  VAL U 125   N  VAL U 110           
SHEET    1 AE2 2 CYS U 165  PRO U 167  0                                        
SHEET    2 AE2 2 CYS U 194  CYS U 196 -1  O  ALA U 195   N  ARG U 166           
SHEET    1 AE3 2 GLU U 173  LEU U 177  0                                        
SHEET    2 AE3 2 TYR U 183  HIS U 187 -1  O  VAL U 186   N  VAL U 174           
SHEET    1 AE4 2 GLY V 104  ARG V 111  0                                        
SHEET    2 AE4 2 THR V 124  ALA V 131 -1  O  VAL V 125   N  VAL V 110           
SHEET    1 AE5 2 CYS V 165  PRO V 167  0                                        
SHEET    2 AE5 2 CYS V 194  CYS V 196 -1  O  ALA V 195   N  ARG V 166           
SHEET    1 AE6 2 GLU V 173  LEU V 177  0                                        
SHEET    2 AE6 2 TYR V 183  HIS V 187 -1  O  HIS V 184   N  PHE V 176           
SHEET    1 AE7 2 ASN W 308  TYR W 309  0                                        
SHEET    2 AE7 2 VAL W 319  SER W 320 -1  O  SER W 320   N  ASN W 308           
SHEET    1 AE8 2 TYR Y  30  PHE Y  31  0                                        
SHEET    2 AE8 2 ALA Y  55  LEU Y  56 -1  O  LEU Y  56   N  TYR Y  30           
SHEET    1 AE9 3 ALA Y  35  TYR Y  36  0                                        
SHEET    2 AE9 3 ALA Y 143  PHE Y 149  1  O  TYR Y 146   N  TYR Y  36           
SHEET    3 AE9 3 LYS Y  39  LEU Y  40  1  N  LEU Y  40   O  SER Y 148           
SHEET    1 AF1 4 ALA Y  35  TYR Y  36  0                                        
SHEET    2 AF1 4 ALA Y 143  PHE Y 149  1  O  TYR Y 146   N  TYR Y  36           
SHEET    3 AF1 4 THR Y 120  PHE Y 126 -1  N  VAL Y 121   O  PHE Y 147           
SHEET    4 AF1 4 ARG Y  67  LEU Y  68 -1  N  ARG Y  67   O  PHE Y 126           
SHEET    1 AF2 3 PRO Y  49  TYR Y  52  0                                        
SHEET    2 AF2 3 LEU Y  94  LEU Y  97 -1  O  LEU Y  95   N  LEU Y  50           
SHEET    3 AF2 3 ILE Y  86  GLN Y  89 -1  N  CYS Y  87   O  TYR Y  96           
SHEET    1 AF3 2 LEU Y  72  TYR Y  73  0                                        
SHEET    2 AF3 2 ARG Y  79  HIS Y  81 -1  O  HIS Y  81   N  LEU Y  72           
SHEET    1 AF4 4 PHE Y 174  ILE Y 176  0                                        
SHEET    2 AF4 4 GLU Y 252  VAL Y 262  1  O  THR Y 261   N  ILE Y 176           
SHEET    3 AF4 4 LYS Y 236  VAL Y 245 -1  N  ALA Y 241   O  VAL Y 256           
SHEET    4 AF4 4 VAL Y 202  ARG Y 205 -1  N  ARG Y 205   O  VAL Y 242           
SHEET    1 AF5 3 THR Y 184  GLN Y 187  0                                        
SHEET    2 AF5 3 GLU Y 222  THR Y 225 -1  O  VAL Y 223   N  HIS Y 186           
SHEET    3 AF5 3 PHE Y 214  CYS Y 216 -1  N  ARG Y 215   O  SER Y 224           
SHEET    1 AF6 4 SER Y 280  VAL Y 283  0                                        
SHEET    2 AF6 4 VAL Y 388  VAL Y 397  1  O  ASN Y 394   N  ALA Y 281           
SHEET    3 AF6 4 ARG Y 368  ASP Y 378 -1  N  MET Y 370   O  VAL Y 395           
SHEET    4 AF6 4 TYR Y 314  LEU Y 318 -1  N  THR Y 317   O  LEU Y 375           
SHEET    1 AF7 3 VAL Y 292  ASP Y 300  0                                        
SHEET    2 AF7 3 VAL Y 347  LEU Y 358 -1  O  LEU Y 356   N  VAL Y 293           
SHEET    3 AF7 3 PHE Y 329  VAL Y 340 -1  N  GLU Y 332   O  ARG Y 355           
SHEET    1 AF8 4 LEU Y 410  SER Y 413  0                                        
SHEET    2 AF8 4 ALA Y 496  GLU Y 505  1  O  GLU Y 505   N  VAL Y 412           
SHEET    3 AF8 4 GLU Y 480  ALA Y 487 -1  N  TYR Y 483   O  LEU Y 500           
SHEET    4 AF8 4 TYR Y 440  LYS Y 441 -1  N  LYS Y 441   O  VAL Y 486           
SHEET    1 AF9 3 GLN Y 421  VAL Y 425  0                                        
SHEET    2 AF9 3 SER Y 462  VAL Y 467 -1  O  LEU Y 465   N  GLY Y 423           
SHEET    3 AF9 3 LEU Y 452  SER Y 457 -1  N  SER Y 457   O  SER Y 462           
SHEET    1 AG1 2 GLU Y 542  ARG Y 544  0                                        
SHEET    2 AG1 2 THR Y 557  SER Y 559 -1  O  SER Y 559   N  GLU Y 542           
SHEET    1 AG2 3 SER Y 589  VAL Y 591  0                                        
SHEET    2 AG2 3 LYS Y 617  GLU Y 621  1  O  CYS Y 618   N  VAL Y 591           
SHEET    3 AG2 3 THR Y 608  PHE Y 612 -1  N  ASN Y 610   O  PHE Y 619           
SHEET    1 AG3 2 GLU Y 595  PRO Y 596  0                                        
SHEET    2 AG3 2 ILE Y 602  ALA Y 604 -1  O  ALA Y 604   N  GLU Y 595           
SHEET    1 AG4 2 ASN X 308  TYR X 309  0                                        
SHEET    2 AG4 2 VAL X 319  SER X 320 -1  O  SER X 320   N  ASN X 308           
SHEET    1 AG5 2 TYR Z  30  PHE Z  31  0                                        
SHEET    2 AG5 2 ALA Z  55  LEU Z  56 -1  O  LEU Z  56   N  TYR Z  30           
SHEET    1 AG6 3 ALA Z  35  TYR Z  36  0                                        
SHEET    2 AG6 3 ALA Z 143  PHE Z 149  1  O  TYR Z 146   N  TYR Z  36           
SHEET    3 AG6 3 LYS Z  39  LEU Z  40  1  N  LEU Z  40   O  SER Z 148           
SHEET    1 AG7 4 ALA Z  35  TYR Z  36  0                                        
SHEET    2 AG7 4 ALA Z 143  PHE Z 149  1  O  TYR Z 146   N  TYR Z  36           
SHEET    3 AG7 4 THR Z 120  PHE Z 126 -1  N  VAL Z 121   O  PHE Z 147           
SHEET    4 AG7 4 ARG Z  67  LEU Z  68 -1  N  ARG Z  67   O  PHE Z 126           
SHEET    1 AG8 3 PRO Z  49  TYR Z  52  0                                        
SHEET    2 AG8 3 LEU Z  94  LEU Z  97 -1  O  LEU Z  95   N  LEU Z  50           
SHEET    3 AG8 3 ILE Z  86  GLN Z  89 -1  N  CYS Z  87   O  TYR Z  96           
SHEET    1 AG9 2 LEU Z  72  TYR Z  73  0                                        
SHEET    2 AG9 2 ARG Z  79  HIS Z  81 -1  O  HIS Z  81   N  LEU Z  72           
SHEET    1 AH1 4 PHE Z 174  ILE Z 176  0                                        
SHEET    2 AH1 4 GLU Z 252  VAL Z 262  1  O  THR Z 261   N  ILE Z 176           
SHEET    3 AH1 4 LYS Z 236  VAL Z 245 -1  N  ALA Z 241   O  VAL Z 256           
SHEET    4 AH1 4 VAL Z 202  ARG Z 205 -1  N  ARG Z 205   O  VAL Z 242           
SHEET    1 AH2 3 THR Z 184  GLN Z 187  0                                        
SHEET    2 AH2 3 GLU Z 222  THR Z 225 -1  O  VAL Z 223   N  HIS Z 186           
SHEET    3 AH2 3 PHE Z 214  CYS Z 216 -1  N  ARG Z 215   O  SER Z 224           
SHEET    1 AH3 4 SER Z 280  VAL Z 283  0                                        
SHEET    2 AH3 4 VAL Z 388  VAL Z 397  1  O  ASN Z 394   N  ALA Z 281           
SHEET    3 AH3 4 ARG Z 368  ASP Z 378 -1  N  MET Z 370   O  VAL Z 395           
SHEET    4 AH3 4 TYR Z 314  LEU Z 318 -1  N  THR Z 317   O  LEU Z 375           
SHEET    1 AH4 3 VAL Z 292  ASP Z 300  0                                        
SHEET    2 AH4 3 VAL Z 347  LEU Z 358 -1  O  LEU Z 356   N  VAL Z 293           
SHEET    3 AH4 3 PHE Z 329  VAL Z 340 -1  N  GLU Z 332   O  ARG Z 355           
SHEET    1 AH5 4 LEU Z 410  SER Z 413  0                                        
SHEET    2 AH5 4 ALA Z 496  GLU Z 505  1  O  GLU Z 505   N  VAL Z 412           
SHEET    3 AH5 4 GLU Z 480  ALA Z 487 -1  N  TYR Z 483   O  LEU Z 500           
SHEET    4 AH5 4 TYR Z 440  LYS Z 441 -1  N  LYS Z 441   O  VAL Z 486           
SHEET    1 AH6 3 GLN Z 421  VAL Z 425  0                                        
SHEET    2 AH6 3 SER Z 462  VAL Z 467 -1  O  LEU Z 465   N  GLY Z 423           
SHEET    3 AH6 3 LEU Z 452  SER Z 457 -1  N  SER Z 457   O  SER Z 462           
SHEET    1 AH7 2 GLU Z 542  ARG Z 544  0                                        
SHEET    2 AH7 2 THR Z 557  SER Z 559 -1  O  SER Z 559   N  GLU Z 542           
SHEET    1 AH8 3 SER Z 589  VAL Z 591  0                                        
SHEET    2 AH8 3 LYS Z 617  GLU Z 621  1  O  CYS Z 618   N  VAL Z 591           
SHEET    3 AH8 3 THR Z 608  PHE Z 612 -1  N  ASN Z 610   O  PHE Z 619           
SHEET    1 AH9 2 GLU Z 595  PRO Z 596  0                                        
SHEET    2 AH9 2 ILE Z 602  ALA Z 604 -1  O  ALA Z 604   N  GLU Z 595           
SSBOND   1 CYS A  103    CYS A  165                          1555   1555  2.03  
SSBOND   2 CYS A  130    CYS A  194                          1555   1555  2.03  
SSBOND   3 CYS A  134    CYS A  196                          1555   1555  2.03  
SSBOND   4 CYS A  164    CYS B  164                          1555   1555  1.96  
SSBOND   5 CYS B  103    CYS B  165                          1555   1555  2.03  
SSBOND   6 CYS B  130    CYS B  194                          1555   1555  2.03  
SSBOND   7 CYS B  134    CYS B  196                          1555   1555  2.03  
SSBOND   8 CYS C   40    CYS C   93                          1555   1555  2.04  
SSBOND   9 CYS C   95    CYS C  105                          1555   1555  2.03  
SSBOND  10 CYS C  161    CYS C  222                          1555   1555  2.02  
SSBOND  11 CYS C  168    CYS C  174                          1555   1555  2.02  
SSBOND  12 CYS C  185    CYS C  200                          1555   1555  2.02  
SSBOND  13 CYS C  195    CYS C  241                          1555   1555  2.02  
SSBOND  14 CYS C  224    CYS C  229                          1555   1555  2.03  
SSBOND  15 CYS C  251    CYS C  323                          1555   1555  2.03  
SSBOND  16 CYS C  258    CYS C  264                          1555   1555  2.03  
SSBOND  17 CYS C  275    CYS C  293                          1555   1555  2.03  
SSBOND  18 CYS C  285    CYS C  347                          1555   1555  2.03  
SSBOND  19 CYS E  137    CYS E  142                          1555   1555  2.03  
SSBOND  20 CYS E  157    CYS E  197                          1555   1555  2.03  
SSBOND  21 CYS E  166    CYS E  243                          1555   1555  2.03  
SSBOND  22 CYS E  426    CYS E  430                          1555   1555  2.03  
SSBOND  23 CYS E  449    CYS E  478                          1555   1555  2.03  
SSBOND  24 CYS E  515    CYS E  531                          1555   1555  2.03  
SSBOND  25 CYS E  519    CYS E  541                          1555   1555  2.03  
SSBOND  26 CYS E  528    CYS E  558                          1555   1555  2.03  
SSBOND  27 CYS E  565    CYS E  581                          1555   1555  2.03  
SSBOND  28 CYS E  570    CYS E  585                          1555   1555  2.03  
SSBOND  29 CYS E  609    CYS E  620                          1555   1555  2.03  
SSBOND  30 CYS E  611    CYS E  618                          1555   1555  2.03  
SSBOND  31 CYS D   40    CYS D   93                          1555   1555  2.04  
SSBOND  32 CYS D   95    CYS D  105                          1555   1555  2.03  
SSBOND  33 CYS D  161    CYS D  222                          1555   1555  2.02  
SSBOND  34 CYS D  168    CYS D  174                          1555   1555  2.02  
SSBOND  35 CYS D  185    CYS D  200                          1555   1555  2.02  
SSBOND  36 CYS D  195    CYS D  241                          1555   1555  2.02  
SSBOND  37 CYS D  224    CYS D  229                          1555   1555  2.03  
SSBOND  38 CYS D  251    CYS D  323                          1555   1555  2.03  
SSBOND  39 CYS D  258    CYS D  264                          1555   1555  2.03  
SSBOND  40 CYS D  275    CYS D  293                          1555   1555  2.03  
SSBOND  41 CYS D  285    CYS D  347                          1555   1555  2.03  
SSBOND  42 CYS F  137    CYS F  142                          1555   1555  2.03  
SSBOND  43 CYS F  157    CYS F  197                          1555   1555  2.03  
SSBOND  44 CYS F  166    CYS F  243                          1555   1555  2.03  
SSBOND  45 CYS F  426    CYS F  430                          1555   1555  2.03  
SSBOND  46 CYS F  449    CYS F  478                          1555   1555  2.03  
SSBOND  47 CYS F  515    CYS F  531                          1555   1555  2.03  
SSBOND  48 CYS F  519    CYS F  541                          1555   1555  2.03  
SSBOND  49 CYS F  528    CYS F  558                          1555   1555  2.03  
SSBOND  50 CYS F  565    CYS F  581                          1555   1555  2.03  
SSBOND  51 CYS F  570    CYS F  585                          1555   1555  2.03  
SSBOND  52 CYS F  609    CYS F  620                          1555   1555  2.03  
SSBOND  53 CYS F  611    CYS F  618                          1555   1555  2.03  
SSBOND  54 CYS U  103    CYS U  165                          1555   1555  2.03  
SSBOND  55 CYS U  130    CYS U  194                          1555   1555  2.03  
SSBOND  56 CYS U  134    CYS U  196                          1555   1555  2.03  
SSBOND  57 CYS U  164    CYS V  164                          1555   1555  2.10  
SSBOND  58 CYS V  103    CYS V  165                          1555   1555  2.03  
SSBOND  59 CYS V  130    CYS V  194                          1555   1555  2.03  
SSBOND  60 CYS V  134    CYS V  196                          1555   1555  2.03  
SSBOND  61 CYS W   40    CYS W   93                          1555   1555  2.04  
SSBOND  62 CYS W   95    CYS W  105                          1555   1555  2.03  
SSBOND  63 CYS W  161    CYS W  222                          1555   1555  2.02  
SSBOND  64 CYS W  168    CYS W  174                          1555   1555  2.03  
SSBOND  65 CYS W  185    CYS W  200                          1555   1555  2.02  
SSBOND  66 CYS W  195    CYS W  241                          1555   1555  2.02  
SSBOND  67 CYS W  224    CYS W  229                          1555   1555  2.03  
SSBOND  68 CYS W  251    CYS W  323                          1555   1555  2.03  
SSBOND  69 CYS W  258    CYS W  264                          1555   1555  2.03  
SSBOND  70 CYS W  275    CYS W  293                          1555   1555  2.03  
SSBOND  71 CYS W  285    CYS W  347                          1555   1555  2.03  
SSBOND  72 CYS Y  137    CYS Y  142                          1555   1555  2.03  
SSBOND  73 CYS Y  157    CYS Y  197                          1555   1555  2.03  
SSBOND  74 CYS Y  166    CYS Y  243                          1555   1555  2.03  
SSBOND  75 CYS Y  426    CYS Y  430                          1555   1555  2.03  
SSBOND  76 CYS Y  449    CYS Y  478                          1555   1555  2.03  
SSBOND  77 CYS Y  515    CYS Y  531                          1555   1555  2.03  
SSBOND  78 CYS Y  519    CYS Y  541                          1555   1555  2.03  
SSBOND  79 CYS Y  528    CYS Y  558                          1555   1555  2.03  
SSBOND  80 CYS Y  565    CYS Y  581                          1555   1555  2.03  
SSBOND  81 CYS Y  570    CYS Y  585                          1555   1555  2.03  
SSBOND  82 CYS Y  609    CYS Y  620                          1555   1555  2.03  
SSBOND  83 CYS Y  611    CYS Y  618                          1555   1555  2.03  
SSBOND  84 CYS X   40    CYS X   93                          1555   1555  2.04  
SSBOND  85 CYS X   95    CYS X  105                          1555   1555  2.03  
SSBOND  86 CYS X  161    CYS X  222                          1555   1555  2.02  
SSBOND  87 CYS X  168    CYS X  174                          1555   1555  2.02  
SSBOND  88 CYS X  185    CYS X  200                          1555   1555  2.02  
SSBOND  89 CYS X  195    CYS X  241                          1555   1555  2.03  
SSBOND  90 CYS X  224    CYS X  229                          1555   1555  2.03  
SSBOND  91 CYS X  251    CYS X  323                          1555   1555  2.03  
SSBOND  92 CYS X  258    CYS X  264                          1555   1555  2.03  
SSBOND  93 CYS X  275    CYS X  293                          1555   1555  2.03  
SSBOND  94 CYS X  285    CYS X  347                          1555   1555  2.03  
SSBOND  95 CYS Z  137    CYS Z  142                          1555   1555  2.03  
SSBOND  96 CYS Z  157    CYS Z  197                          1555   1555  2.03  
SSBOND  97 CYS Z  166    CYS Z  243                          1555   1555  2.03  
SSBOND  98 CYS Z  426    CYS Z  430                          1555   1555  2.03  
SSBOND  99 CYS Z  449    CYS Z  478                          1555   1555  2.03  
SSBOND 100 CYS Z  515    CYS Z  531                          1555   1555  2.03  
SSBOND 101 CYS Z  519    CYS Z  541                          1555   1555  2.03  
SSBOND 102 CYS Z  528    CYS Z  558                          1555   1555  2.03  
SSBOND 103 CYS Z  565    CYS Z  581                          1555   1555  2.03  
SSBOND 104 CYS Z  570    CYS Z  585                          1555   1555  2.03  
SSBOND 105 CYS Z  609    CYS Z  620                          1555   1555  2.03  
SSBOND 106 CYS Z  611    CYS Z  618                          1555   1555  2.03  
LINK         ND2 ASN E 336                 C1  NAG E2009     1555   1555  1.44  
LINK         ND2 ASN E 361                 C1  NAG E2010     1555   1555  1.43  
LINK         ND2 ASN E 367                 C1  NAG E2008     1555   1555  1.44  
LINK         ND2 ASN E 377                 C1  NAG E2005     1555   1555  1.44  
LINK         ND2 ASN E 394                 C1  NAG E2006     1555   1555  1.44  
LINK         ND2 ASN E 468                 C1  NAG E2007     1555   1555  1.43  
LINK         ND2 ASN F 336                 C1  NAG F2009     1555   1555  1.44  
LINK         ND2 ASN F 361                 C1  NAG F2010     1555   1555  1.43  
LINK         ND2 ASN F 367                 C1  NAG F2008     1555   1555  1.44  
LINK         ND2 ASN F 377                 C1  NAG F2005     1555   1555  1.44  
LINK         ND2 ASN F 394                 C1  NAG F2006     1555   1555  1.44  
LINK         ND2 ASN F 468                 C1  NAG F2007     1555   1555  1.43  
LINK         ND2 ASN Y 336                 C1  NAG Y2009     1555   1555  1.44  
LINK         ND2 ASN Y 361                 C1  NAG Y2010     1555   1555  1.44  
LINK         ND2 ASN Y 367                 C1  NAG Y2008     1555   1555  1.44  
LINK         ND2 ASN Y 377                 C1  NAG Y2005     1555   1555  1.44  
LINK         ND2 ASN Y 394                 C1  NAG Y2006     1555   1555  1.44  
LINK         ND2 ASN Y 468                 C1  NAG Y2007     1555   1555  1.43  
LINK         ND2 ASN Z 336                 C1  NAG Z2009     1555   1555  1.44  
LINK         ND2 ASN Z 361                 C1  NAG Z2010     1555   1555  1.44  
LINK         ND2 ASN Z 367                 C1  NAG Z2008     1555   1555  1.44  
LINK         ND2 ASN Z 377                 C1  NAG Z2005     1555   1555  1.44  
LINK         ND2 ASN Z 394                 C1  NAG Z2006     1555   1555  1.44  
LINK         ND2 ASN Z 468                 C1  NAG Z2007     1555   1555  1.44  
LINK         OE1 GLU E 178                CA    CA E2001     1555   1555  2.35  
LINK         OE2 GLU E 178                CA    CA E2001     1555   1555  2.39  
LINK         OD1 ASN E 179                CA    CA E2001     1555   1555  2.33  
LINK         OD1 ASP E 230                CA    CA E2001     1555   1555  2.20  
LINK         OD2 ASP E 230                CA    CA E2001     1555   1555  2.39  
LINK         OE1 GLU E 232                CA    CA E2001     1555   1555  2.44  
LINK         OE2 GLU E 232                CA    CA E2002     1555   1555  2.37  
LINK         OD1 ASP E 264                CA    CA E2002     1555   1555  2.32  
LINK         OD2 ASP E 264                CA    CA E2002     1555   1555  2.37  
LINK         O   GLU E 265                CA    CA E2002     1555   1555  2.41  
LINK         OD1 ASP E 266                CA    CA E2003     1555   1555  2.61  
LINK         OD2 ASP E 267                CA    CA E2001     1555   1555  2.21  
LINK         OD1 ASP E 267                CA    CA E2002     1555   1555  2.33  
LINK         O   SER E 268                CA    CA E2003     1555   1555  2.57  
LINK         OD1 ASP E 300                CA    CA E2003     1555   1555  2.67  
LINK         OD2 ASP E 300                CA    CA E2003     1555   1555  2.27  
LINK         OD1 ASP E 302                CA    CA E2002     1555   1555  2.36  
LINK         OD2 ASP E 302                CA    CA E2003     1555   1555  2.20  
LINK         OH  TYR E 314                CA    CA E2003     1555   1555  2.39  
LINK         OD1 ASP E 378                CA    CA E2003     1555   1555  2.76  
LINK         OD2 ASP E 378                CA    CA E2003     1555   1555  2.26  
LINK         O   THR E 564                CA    CA E2004     1555   1555  2.37  
LINK         OD1 ASP E 567                CA    CA E2004     1555   1555  2.32  
LINK         OD2 ASP E 567                CA    CA E2004     1555   1555  2.37  
LINK         O   HIS E 569                CA    CA E2004     1555   1555  2.44  
LINK         OE1 GLU E 574                CA    CA E2004     1555   1555  2.36  
LINK         OE2 GLU E 574                CA    CA E2004     1555   1555  2.38  
LINK         OD2 ASP E 584                CA    CA E2004     1555   1555  2.40  
LINK         OE1 GLU F 178                CA    CA F2001     1555   1555  2.35  
LINK         OE2 GLU F 178                CA    CA F2001     1555   1555  2.39  
LINK         OD1 ASN F 179                CA    CA F2001     1555   1555  2.33  
LINK         OD1 ASP F 230                CA    CA F2001     1555   1555  2.20  
LINK         OD2 ASP F 230                CA    CA F2001     1555   1555  2.39  
LINK         OE1 GLU F 232                CA    CA F2001     1555   1555  2.44  
LINK         OE2 GLU F 232                CA    CA F2002     1555   1555  2.37  
LINK         OD1 ASP F 264                CA    CA F2002     1555   1555  2.32  
LINK         OD2 ASP F 264                CA    CA F2002     1555   1555  2.37  
LINK         O   GLU F 265                CA    CA F2002     1555   1555  2.41  
LINK         OD1 ASP F 266                CA    CA F2003     1555   1555  2.61  
LINK         OD2 ASP F 267                CA    CA F2001     1555   1555  2.21  
LINK         OD1 ASP F 267                CA    CA F2002     1555   1555  2.33  
LINK         O   SER F 268                CA    CA F2003     1555   1555  2.57  
LINK         OD1 ASP F 300                CA    CA F2003     1555   1555  2.68  
LINK         OD2 ASP F 300                CA    CA F2003     1555   1555  2.27  
LINK         OD1 ASP F 302                CA    CA F2002     1555   1555  2.36  
LINK         OD2 ASP F 302                CA    CA F2003     1555   1555  2.20  
LINK         OH  TYR F 314                CA    CA F2003     1555   1555  2.39  
LINK         OD1 ASP F 378                CA    CA F2003     1555   1555  2.76  
LINK         OD2 ASP F 378                CA    CA F2003     1555   1555  2.26  
LINK         O   THR F 564                CA    CA F2004     1555   1555  2.37  
LINK         OD1 ASP F 567                CA    CA F2004     1555   1555  2.32  
LINK         OD2 ASP F 567                CA    CA F2004     1555   1555  2.37  
LINK         O   HIS F 569                CA    CA F2004     1555   1555  2.44  
LINK         OE1 GLU F 574                CA    CA F2004     1555   1555  2.36  
LINK         OE2 GLU F 574                CA    CA F2004     1555   1555  2.38  
LINK         OD2 ASP F 584                CA    CA F2004     1555   1555  2.40  
LINK         OE1 GLU Y 178                CA    CA Y2001     1555   1555  2.35  
LINK         OE2 GLU Y 178                CA    CA Y2001     1555   1555  2.39  
LINK         OD1 ASN Y 179                CA    CA Y2001     1555   1555  2.33  
LINK         OD1 ASP Y 230                CA    CA Y2001     1555   1555  2.20  
LINK         OD2 ASP Y 230                CA    CA Y2001     1555   1555  2.39  
LINK         OE1 GLU Y 232                CA    CA Y2001     1555   1555  2.44  
LINK         OE2 GLU Y 232                CA    CA Y2002     1555   1555  2.37  
LINK         OD1 ASP Y 264                CA    CA Y2002     1555   1555  2.32  
LINK         OD2 ASP Y 264                CA    CA Y2002     1555   1555  2.37  
LINK         O   GLU Y 265                CA    CA Y2002     1555   1555  2.41  
LINK         OD1 ASP Y 266                CA    CA Y2003     1555   1555  2.61  
LINK         OD2 ASP Y 267                CA    CA Y2001     1555   1555  2.21  
LINK         OD1 ASP Y 267                CA    CA Y2002     1555   1555  2.33  
LINK         O   SER Y 268                CA    CA Y2003     1555   1555  2.57  
LINK         OD1 ASP Y 300                CA    CA Y2003     1555   1555  2.67  
LINK         OD2 ASP Y 300                CA    CA Y2003     1555   1555  2.27  
LINK         OD1 ASP Y 302                CA    CA Y2002     1555   1555  2.36  
LINK         OD2 ASP Y 302                CA    CA Y2003     1555   1555  2.20  
LINK         OH  TYR Y 314                CA    CA Y2003     1555   1555  2.39  
LINK         OD1 ASP Y 378                CA    CA Y2003     1555   1555  2.76  
LINK         OD2 ASP Y 378                CA    CA Y2003     1555   1555  2.26  
LINK         O   THR Y 564                CA    CA Y2004     1555   1555  2.37  
LINK         OD1 ASP Y 567                CA    CA Y2004     1555   1555  2.32  
LINK         OD2 ASP Y 567                CA    CA Y2004     1555   1555  2.36  
LINK         O   HIS Y 569                CA    CA Y2004     1555   1555  2.44  
LINK         OE1 GLU Y 574                CA    CA Y2004     1555   1555  2.37  
LINK         OE2 GLU Y 574                CA    CA Y2004     1555   1555  2.38  
LINK         OD2 ASP Y 584                CA    CA Y2004     1555   1555  2.40  
LINK         OE1 GLU Z 178                CA    CA Z2001     1555   1555  2.35  
LINK         OE2 GLU Z 178                CA    CA Z2001     1555   1555  2.39  
LINK         OD1 ASN Z 179                CA    CA Z2001     1555   1555  2.33  
LINK         OD1 ASP Z 230                CA    CA Z2001     1555   1555  2.20  
LINK         OD2 ASP Z 230                CA    CA Z2001     1555   1555  2.39  
LINK         OE1 GLU Z 232                CA    CA Z2001     1555   1555  2.44  
LINK         OE2 GLU Z 232                CA    CA Z2002     1555   1555  2.37  
LINK         OD1 ASP Z 264                CA    CA Z2002     1555   1555  2.32  
LINK         OD2 ASP Z 264                CA    CA Z2002     1555   1555  2.37  
LINK         O   GLU Z 265                CA    CA Z2002     1555   1555  2.41  
LINK         OD1 ASP Z 266                CA    CA Z2003     1555   1555  2.61  
LINK         OD2 ASP Z 267                CA    CA Z2001     1555   1555  2.21  
LINK         OD1 ASP Z 267                CA    CA Z2002     1555   1555  2.33  
LINK         O   SER Z 268                CA    CA Z2003     1555   1555  2.57  
LINK         OD1 ASP Z 300                CA    CA Z2003     1555   1555  2.67  
LINK         OD2 ASP Z 300                CA    CA Z2003     1555   1555  2.27  
LINK         OD1 ASP Z 302                CA    CA Z2002     1555   1555  2.36  
LINK         OD2 ASP Z 302                CA    CA Z2003     1555   1555  2.20  
LINK         OH  TYR Z 314                CA    CA Z2003     1555   1555  2.39  
LINK         OD1 ASP Z 378                CA    CA Z2003     1555   1555  2.76  
LINK         OD2 ASP Z 378                CA    CA Z2003     1555   1555  2.26  
LINK         O   THR Z 564                CA    CA Z2004     1555   1555  2.37  
LINK         OD1 ASP Z 567                CA    CA Z2004     1555   1555  2.32  
LINK         OD2 ASP Z 567                CA    CA Z2004     1555   1555  2.36  
LINK         O   HIS Z 569                CA    CA Z2004     1555   1555  2.44  
LINK         OE1 GLU Z 574                CA    CA Z2004     1555   1555  2.37  
LINK         OE2 GLU Z 574                CA    CA Z2004     1555   1555  2.38  
LINK         OD2 ASP Z 584                CA    CA Z2004     1555   1555  2.40  
CISPEP   1 TRP E  139    PRO E  140          0        -5.24                     
CISPEP   2 TRP F  139    PRO F  140          0        -5.28                     
CISPEP   3 TRP Y  139    PRO Y  140          0        -5.30                     
CISPEP   4 TRP Z  139    PRO Z  140          0        -5.35                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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