GenomeNet

Database: PDB
Entry: 6BQN
LinkDB: 6BQN
Original site: 6BQN 
HEADER    MEMBRANE PROTEIN                        28-NOV-17   6BQN              
TITLE     CRYO-EM STRUCTURE OF ENAC                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SCNN1A;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: TRANSMEMBRANE HELICES HAVE BEEN BUILT WITH POLY UNK   
COMPND   6 SINCE THE DENSITY FOR THE TRANSMEMBRANE DOMAIN IS NOT GOOD ENOUGH TO 
COMPND   7 ACCURATELY BUILD A MODEL. RESIDUES THAT HAVE NOT BEEN BUILT IS DUE TO
COMPND   8 FLEXIBLE AREAS OF THE PROTEIN WHERE DENSITY IS MISSING. THE FULL     
COMPND   9 SEQUENCE IS DESCRIBED IN SEQUENCE DETAILS.;                          
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: SCNN1B;                                                    
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: TRANSMEMBRANE HELICES HAVE BEEN BUILT WITH POLY UNK   
COMPND  15 SINCE THE DENSITY FOR THE TRANSMEMBRANE DOMAIN IS NOT GOOD ENOUGH TO 
COMPND  16 ACCURATELY BUILD A MODEL. RESIDUES THAT HAVE NOT BEEN BUILT IS DUE TO
COMPND  17 FLEXIBLE AREAS OF THE PROTEIN WHERE DENSITY IS MISSING. THE FULL     
COMPND  18 SEQUENCE IS DESCRIBED IN SEQUENCE DETAILS.;                          
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: EGFP-SCNN1G CHIMERA;                                       
COMPND  21 CHAIN: C;                                                            
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 OTHER_DETAILS: THE PROTEIN IS EGFP-SCNN1G CHIMERA. TRANSMEMBRANE     
COMPND  24 HELICES HAVE BEEN BUILT WITH POLY UNK SINCE THE DENSITY FOR THE      
COMPND  25 TRANSMEMBRANE DOMAIN IS NOT GOOD ENOUGH TO ACCURATELY BUILD A MODEL. 
COMPND  26 RESIDUES THAT HAVE NOT BEEN BUILT IS DUE TO FLEXIBLE AREAS OF THE    
COMPND  27 PROTEIN WHERE DENSITY IS MISSING. THE FIRST 260 RESIDUES IS A HIS8   
COMPND  28 TAG AND A STREP-TAG FOLLOWED BY EGFP (UNIPROT ACCESSION CODE:        
COMPND  29 C5MKY7). THE FULL SEQUENCE IS DESCRIBED IN SEQUENCE DETAILS.;        
COMPND  30 MOL_ID: 4;                                                           
COMPND  31 MOLECULE: 7B1 FAB;                                                   
COMPND  32 CHAIN: D;                                                            
COMPND  33 OTHER_DETAILS: SEQUENCE UNKNOWN, BUILT WITH POLY UNK.;               
COMPND  34 MOL_ID: 5;                                                           
COMPND  35 MOLECULE: 7B1 FAB;                                                   
COMPND  36 CHAIN: E;                                                            
COMPND  37 OTHER_DETAILS: SEQUENCE UNKNOWN, BUILT WITH POLY UNK.;               
COMPND  38 MOL_ID: 6;                                                           
COMPND  39 MOLECULE: 10D4 FAB;                                                  
COMPND  40 CHAIN: F;                                                            
COMPND  41 OTHER_DETAILS: SEQUENCE UNKNOWN, BUILT WITH POLY UNK.;               
COMPND  42 MOL_ID: 7;                                                           
COMPND  43 MOLECULE: 10D4 FAB;                                                  
COMPND  44 CHAIN: G;                                                            
COMPND  45 OTHER_DETAILS: SEQUENCE UNKNOWN, BUILT WITH POLY UNK.                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 MOL_ID: 5;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 MOL_ID: 6;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  29 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  30 ORGANISM_TAXID: 10090;                                               
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  33 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  34 ORGANISM_TAXID: 10090                                                
KEYWDS    SODIUM CHANNEL, MEMBRANE PROTEIN                                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.NORENG,A.BHARADWAJ,R.POSERT,C.YOSHIOKA,I.BACONGUIS                  
REVDAT   3   18-DEC-19 6BQN    1       SCALE                                    
REVDAT   2   24-OCT-18 6BQN    1       COMPND JRNL                              
REVDAT   1   10-OCT-18 6BQN    0                                                
JRNL        AUTH   S.NORENG,A.BHARADWAJ,R.POSERT,C.YOSHIOKA,I.BACONGUIS         
JRNL        TITL   STRUCTURE OF THE HUMAN EPITHELIAL SODIUM CHANNEL BY          
JRNL        TITL 2 CRYO-ELECTRON MICROSCOPY.                                    
JRNL        REF    ELIFE                         V.   7       2018              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   30251954                                                     
JRNL        DOI    10.7554/ELIFE.39340                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
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)  : 3.900                          
REMARK   3   NUMBER OF PARTICLES               : 304615                         
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 6BQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231275.                                   
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                 : MEMBRANE PROTEIN COMPLEX          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
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 SUMMIT (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                        : NULL                           
REMARK 245   IMAGING MODE                      : OTHER                          
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 60.00                          
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
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: HEPTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G                   
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     SER A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     PHE A   167                                                      
REMARK 465     THR A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     VAL A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     ARG A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     ARG A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     ARG A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     VAL A   193                                                      
REMARK 465     PRO A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     PRO A   196                                                      
REMARK 465     PRO A   197                                                      
REMARK 465     HIS A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     VAL A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     LEU A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     ASP A   212                                                      
REMARK 465     ASN A   213                                                      
REMARK 465     ASN A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     GLN A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     ASP A   218                                                      
REMARK 465     TRP A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     ASP A   221                                                      
REMARK 465     TRP A   222                                                      
REMARK 465     GLU B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     SER B   132                                                      
REMARK 465     HIS B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     ASN B   135                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     ASN B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     ASN B   172                                                      
REMARK 465     GLY B   173                                                      
REMARK 465     LEU B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     SER B   178                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     PHE C   131                                                      
REMARK 465     PRO C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     SER C   134                                                      
REMARK 465     ALA C   135                                                      
REMARK 465     ALA C   136                                                      
REMARK 465     ALA C   137                                                      
REMARK 465     ALA C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     ALA C   140                                                      
REMARK 465     GLU C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     TRP C   143                                                      
REMARK 465     ASN C   144                                                      
REMARK 465     SER C   145                                                      
REMARK 465     VAL C   146                                                      
REMARK 465     SER C   147                                                      
REMARK 465     GLU C   148                                                      
REMARK 465     GLY C   149                                                      
REMARK 465     LYS C   150                                                      
REMARK 465     GLN C   151                                                      
REMARK 465     PRO C   152                                                      
REMARK 465     ARG C   153                                                      
REMARK 465     ASP C   164                                                      
REMARK 465     GLN C   165                                                      
REMARK 465     ASP C   166                                                      
REMARK 465     GLU C   167                                                      
REMARK 465     LYS C   168                                                      
REMARK 465     GLY C   169                                                      
REMARK 465     LYS C   170                                                      
REMARK 465     ALA C   171                                                      
REMARK 465     ARG C   172                                                      
REMARK 465     ASP C   173                                                      
REMARK 465     PHE C   174                                                      
REMARK 465     PHE C   175                                                      
REMARK 465     THR C   176                                                      
REMARK 465     GLY C   177                                                      
REMARK 465     GLN C   178                                                      
REMARK 465     GLN C   179                                                      
REMARK 465     GLN C   180                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     VAL C   182                                                      
REMARK 465     GLY C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     SER C   185                                                      
REMARK 465     ILE C   186                                                      
REMARK 465     ILE C   187                                                      
REMARK 465     HIS C   188                                                      
REMARK 465     LYS C   189                                                      
REMARK 465     ALA C   190                                                      
REMARK 465     SER C   191                                                      
REMARK 465     ASN C   192                                                      
REMARK 465     VAL C   193                                                      
REMARK 465     MET C   194                                                      
REMARK 465     HIS C   195                                                      
REMARK 465     ILE C   196                                                      
REMARK 465     GLU C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     LYS C   199                                                      
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   CZ   ARG A   448     O    UNK D    87              2.11            
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    GLN A 291       50.23    -92.60                                   
REMARK 500    ASN A 315       30.92    -96.17                                   
REMARK 500    MET A 362      -10.18     72.52                                   
REMARK 500    MET B 432       57.42    -94.75                                   
REMARK 500    UNK B 519      -51.22   -133.94                                   
REMARK 500    PRO C 104     -164.60    -73.06                                   
REMARK 500    TYR C 105      150.90    -47.80                                   
REMARK 500    VAL C 258      -55.32   -122.04                                   
REMARK 500    SER C 366      -62.44    -96.83                                   
REMARK 500    TYR C 369     -158.77   -144.16                                   
REMARK 500    ASN C 493      -39.52   -130.03                                   
REMARK 500    UNK C 528       30.43    -99.47                                   
REMARK 500    UNK D 100       49.86    -90.68                                   
REMARK 500    UNK D 105       50.01   -118.94                                   
REMARK 500    UNK E 102       10.58   -140.93                                   
REMARK 500    UNK F  53       51.10    -93.41                                   
REMARK 500    UNK F  67       30.35    -96.05                                   
REMARK 500    UNK F 103       51.87    -94.25                                   
REMARK 500    UNK F 106       51.25    -93.59                                   
REMARK 500    UNK G  61     -168.48   -126.78                                   
REMARK 500    UNK G  72       58.08    -94.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-7130   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF ENAC                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF SCNNIA IS                                            
REMARK 999 MAEEEALIEFHRSYRELFEFFANNTTIHGAIRLVSSQHNRMKTAFWAVLWLATFGMMYWQFGLLFGEY 
REMARK 999 FSYPVSLNINLNSDKLVFPAVTICTLNPYRYPEIKEELEELDRITEQTLFDLYKYSSFTTLVAGSRSR 
REMARK 999 ADLRGTLPHPLQALAVPPPPHGAAAAASVASSLRDNNPQVDWKDWKIGFQLCNQNKSDCFYQTYSSGV 
REMARK 999 DAVAEWYAFHYINILSRLPETLPSLEEDTLGNFIFACRFNQVSCNQANYSHFHHPMYGNCYTFNDKNN 
REMARK 999 SNLWMSSMPGINNGLSLMLRAEQNDFIPLLSTVTGARVMVHGQDEPAFMDDGGFNLRPGVETSISMRK 
REMARK 999 ETLDRLGGDYGDCTKNGSDVPVENLYPSKYTQQVCIHSCFQESMIKECGCAYIFYPRPQNVEYCDYRK 
REMARK 999 HSSWGYCYYKLQVDFSSDHLGCFTKCRKPCSVTSYQLSAGYSRWPSVTSQEWVFQMLSRQNNYTVNNK 
REMARK 999 RNGVAKVNIFFKELNYKTNSESPSVTMVTLLSNLGSQWSLWFGSSVLSVVEMAELVFDLLVIM      
REMARK 999 THE SEUQNCE OF SCNN1B IS                                             
REMARK 999 MADNTNTHGPKRIIKEGPKKKAMWFLLTLLFAALVCWQWGIFIRTYLSWEVSVSLSVGFKTMDFPAVT 
REMARK 999 ICNASPFKYSKIKHLLKDLDELMEAVLERILAPELSHANATRNLNFSIWNHTPLVLIDERNPHHPMVL 
REMARK 999 DLFGDNHNGLTSSSASEKICNAHGCKMAMRLCSLNRTQCTFRNFTSATQALTEWYILQATNIFAQVPQ 
REMARK 999 QELVEMSYPGEQMILACLFGAEPCNYRNFTSIFYPHYGNCYIFNWGMTEKALPSANPGTEFGLKLILD 
REMARK 999 IGQEDYVPFLASTAGVRLMLHEQRSYPFIRDEGIYAMSGTETSIGVLVDKLQRMGEPYSPCTVNGSEV 
REMARK 999 PVQNFYSDYNTTYSIQACLRSCFQDHMIRNCNCGHYLYPLPRGEKYCNNRDFPDWAHCYSDLQMSVAQ 
REMARK 999 RETCIGMCKESCNDTQYKMTISMADWPSEASEDWIFHVLSQERDQSTNITLSRKGIVKLNIYFQEFNY 
REMARK 999 RTIEESAANNIVWLLSNLGGQFGFWMGGSVLALIEFGEIIIDFVWITIIKLVALAKS            
REMARK 999 THE SEQUENCE OF EGFP-SCNN1G CHIMERA IS                               
REMARK 999 MHHHHHHHHAAAWSHPQFEKGGSMVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTL 
REMARK 999 KFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYTTRAEV 
REMARK 999 KFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLAD 
REMARK 999 HYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYKSGLRSGLVPR 
REMARK 999 GGRQAPTIKELMRWYALNTNTHGIRRIVVSRGRLRRLLWIGFTLTAVALILWQCALLVFSFYTVSVSI 
REMARK 999 KVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQETREALKSLYGFPESAAAAEAESWNSVSEGKQPR 
REMARK 999 FSHRIPLLIFDQDEKGKARDFFTGQQQQVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSS 
REMARK 999 GINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNR 
REMARK 999 ENETILSTSMGGSEYGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMVTSIGM 
REMARK 999 HLTESFKLSEPYSQCTEDGSDVPIRNIYNAAYSLQICLHSCFQTKMVEKCGCAQYSQPLPPAANYCNY 
REMARK 999 QQHPNWMYCYYQLHRAFVQEELGCQSVCKEACSFKEWTLTTSLAQWPSVVSEKWLLPVLTWDQGRQVN 
REMARK 999 KKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMSCSVVAVIEIIEVFFIDFFSII 
REMARK 999 ARRQWQKAK                                                            
DBREF  6BQN A   78   572  PDB    6BQN     6BQN            78    572             
DBREF  6BQN B   48   542  PDB    6BQN     6BQN            48    542             
DBREF  6BQN C   49   551  PDB    6BQN     6BQN            49    551             
DBREF  6BQN D    1   128  PDB    6BQN     6BQN             1    128             
DBREF  6BQN E    1   122  PDB    6BQN     6BQN             1    122             
DBREF  6BQN F    1   116  PDB    6BQN     6BQN             1    116             
DBREF  6BQN G    1   112  PDB    6BQN     6BQN             1    112             
SEQRES   1 A  489  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 A  489  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 A  489  UNK UNK UNK SER TYR PRO VAL SER LEU ASN ILE ASN LEU          
SEQRES   4 A  489  ASN SER ASP LYS LEU VAL PHE PRO ALA VAL THR ILE CYS          
SEQRES   5 A  489  THR LEU ASN PRO TYR ARG TYR PRO GLU ILE LYS GLU GLU          
SEQRES   6 A  489  LEU GLU GLU LEU ASP ARG ILE THR GLU GLN THR LEU PHE          
SEQRES   7 A  489  ASP LEU TYR LYS TYR SER SER PHE THR THR LEU VAL ALA          
SEQRES   8 A  489  GLY SER ARG SER ARG ALA ASP LEU ARG GLY THR LEU PRO          
SEQRES   9 A  489  HIS PRO LEU GLN ALA LEU ALA VAL PRO PRO PRO PRO HIS          
SEQRES  10 A  489  GLY ALA ALA ALA ALA ALA SER VAL ALA SER SER LEU ARG          
SEQRES  11 A  489  ASP ASN ASN PRO GLN VAL ASP TRP LYS ASP TRP LYS ILE          
SEQRES  12 A  489  GLY PHE GLN LEU CYS ASN GLN ASN LYS SER ASP CYS PHE          
SEQRES  13 A  489  TYR GLN THR TYR SER SER GLY VAL ASP ALA VAL ALA GLU          
SEQRES  14 A  489  TRP TYR ALA PHE HIS TYR ILE ASN ILE LEU SER ARG LEU          
SEQRES  15 A  489  PRO GLU THR LEU PRO SER LEU GLU GLU ASP THR LEU GLY          
SEQRES  16 A  489  ASN PHE ILE PHE ALA CYS ARG PHE ASN GLN VAL SER CYS          
SEQRES  17 A  489  ASN GLN ALA ASN TYR SER HIS PHE HIS HIS PRO MET TYR          
SEQRES  18 A  489  GLY ASN CYS TYR THR PHE ASN ASP LYS ASN ASN SER ASN          
SEQRES  19 A  489  LEU TRP MET SER SER MET PRO GLY ILE ASN ASN GLY LEU          
SEQRES  20 A  489  SER LEU MET LEU ARG ALA GLU GLN ASN ASP PHE ILE PRO          
SEQRES  21 A  489  LEU LEU SER THR VAL THR GLY ALA ARG VAL MET VAL HIS          
SEQRES  22 A  489  GLY GLN ASP GLU PRO ALA PHE MET ASP ASP GLY GLY PHE          
SEQRES  23 A  489  ASN LEU ARG PRO GLY VAL GLU THR SER ILE SER MET ARG          
SEQRES  24 A  489  LYS GLU THR LEU ASP ARG LEU GLY GLY ASP TYR GLY ASP          
SEQRES  25 A  489  CYS THR LYS ASN GLY SER ASP VAL PRO VAL GLU ASN LEU          
SEQRES  26 A  489  TYR PRO SER LYS TYR THR GLN GLN VAL CYS ILE HIS SER          
SEQRES  27 A  489  CYS PHE GLN GLU SER MET ILE LYS GLU CYS GLY CYS ALA          
SEQRES  28 A  489  TYR ILE PHE TYR PRO ARG PRO GLN ASN VAL GLU TYR CYS          
SEQRES  29 A  489  ASP TYR ARG LYS HIS SER SER TRP GLY TYR CYS TYR TYR          
SEQRES  30 A  489  LYS LEU GLN VAL ASP PHE SER SER ASP HIS LEU GLY CYS          
SEQRES  31 A  489  PHE THR LYS CYS ARG LYS PRO CYS SER VAL THR SER TYR          
SEQRES  32 A  489  GLN LEU SER ALA GLY TYR SER ARG TRP PRO SER VAL THR          
SEQRES  33 A  489  SER GLN GLU TRP VAL PHE GLN MET LEU SER ARG GLN ASN          
SEQRES  34 A  489  ASN TYR THR VAL ASN ASN LYS ARG ASN GLY VAL ALA LYS          
SEQRES  35 A  489  VAL ASN ILE PHE PHE LYS GLU LEU ASN TYR LYS THR ASN          
SEQRES  36 A  489  SER GLU SER PRO SER VAL THR UNK UNK UNK UNK UNK UNK          
SEQRES  37 A  489  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  38 A  489  UNK UNK UNK UNK UNK UNK UNK UNK                              
SEQRES   1 B  495  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 B  495  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK THR          
SEQRES   3 B  495  TYR LEU SER TRP GLU VAL SER VAL SER LEU SER VAL GLY          
SEQRES   4 B  495  PHE LYS THR MET ASP PHE PRO ALA VAL THR ILE CYS ASN          
SEQRES   5 B  495  ALA SER PRO PHE LYS TYR SER LYS ILE LYS HIS LEU LEU          
SEQRES   6 B  495  LYS ASP LEU ASP GLU LEU MET GLU ALA VAL LEU GLU ARG          
SEQRES   7 B  495  ILE LEU ALA PRO GLU LEU SER HIS ALA ASN ALA THR ARG          
SEQRES   8 B  495  ASN LEU ASN PHE SER ILE TRP ASN HIS THR PRO LEU VAL          
SEQRES   9 B  495  LEU ILE ASP GLU ARG ASN PRO HIS HIS PRO MET VAL LEU          
SEQRES  10 B  495  ASP LEU PHE GLY ASP ASN HIS ASN GLY LEU THR SER SER          
SEQRES  11 B  495  SER ALA SER GLU LYS ILE CYS ASN ALA HIS GLY CYS LYS          
SEQRES  12 B  495  MET ALA MET ARG LEU CYS SER LEU ASN ARG THR GLN CYS          
SEQRES  13 B  495  THR PHE ARG ASN PHE THR SER ALA THR GLN ALA LEU THR          
SEQRES  14 B  495  GLU TRP TYR ILE LEU GLN ALA THR ASN ILE PHE ALA GLN          
SEQRES  15 B  495  VAL PRO GLN GLN GLU LEU VAL GLU MET SER TYR PRO GLY          
SEQRES  16 B  495  GLU GLN MET ILE LEU ALA CYS LEU PHE GLY ALA GLU PRO          
SEQRES  17 B  495  CYS ASN TYR ARG ASN PHE THR SER ILE PHE TYR PRO HIS          
SEQRES  18 B  495  TYR GLY ASN CYS TYR ILE PHE ASN TRP GLY MET THR GLU          
SEQRES  19 B  495  LYS ALA LEU PRO SER ALA ASN PRO GLY THR GLU PHE GLY          
SEQRES  20 B  495  LEU LYS LEU ILE LEU ASP ILE GLY GLN GLU ASP TYR VAL          
SEQRES  21 B  495  PRO PHE LEU ALA SER THR ALA GLY VAL ARG LEU MET LEU          
SEQRES  22 B  495  HIS GLU GLN ARG SER TYR PRO PHE ILE ARG ASP GLU GLY          
SEQRES  23 B  495  ILE TYR ALA MET SER GLY THR GLU THR SER ILE GLY VAL          
SEQRES  24 B  495  LEU VAL ASP LYS LEU GLN ARG MET GLY GLU PRO TYR SER          
SEQRES  25 B  495  PRO CYS THR VAL ASN GLY SER GLU VAL PRO VAL GLN ASN          
SEQRES  26 B  495  PHE TYR SER ASP TYR ASN THR THR TYR SER ILE GLN ALA          
SEQRES  27 B  495  CYS LEU ARG SER CYS PHE GLN ASP HIS MET ILE ARG ASN          
SEQRES  28 B  495  CYS ASN CYS GLY HIS TYR LEU TYR PRO LEU PRO ARG GLY          
SEQRES  29 B  495  GLU LYS TYR CYS ASN ASN ARG ASP PHE PRO ASP TRP ALA          
SEQRES  30 B  495  HIS CYS TYR SER ASP LEU GLN MET SER VAL ALA GLN ARG          
SEQRES  31 B  495  GLU THR CYS ILE GLY MET CYS LYS GLU SER CYS ASN ASP          
SEQRES  32 B  495  THR GLN TYR LYS MET THR ILE SER MET ALA ASP TRP PRO          
SEQRES  33 B  495  SER GLU ALA SER GLU ASP TRP ILE PHE HIS VAL LEU SER          
SEQRES  34 B  495  GLN GLU ARG ASP GLN SER THR ASN ILE THR LEU SER ARG          
SEQRES  35 B  495  LYS GLY ILE VAL LYS LEU ASN ILE TYR PHE GLN GLU PHE          
SEQRES  36 B  495  ASN TYR ARG THR ILE GLU GLU SER ALA ALA ASN ASN ILE          
SEQRES  37 B  495  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  38 B  495  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  39 B  495  UNK                                                          
SEQRES   1 C  503  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 C  503  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 C  503  UNK UNK UNK PHE TYR THR VAL SER VAL SER ILE LYS VAL          
SEQRES   4 C  503  HIS PHE ARG LYS LEU ASP PHE PRO ALA VAL THR ILE CYS          
SEQRES   5 C  503  ASN ILE ASN PRO TYR LYS TYR SER THR VAL ARG HIS LEU          
SEQRES   6 C  503  LEU ALA ASP LEU GLU GLN GLU THR ARG GLU ALA LEU LYS          
SEQRES   7 C  503  SER LEU TYR GLY PHE PRO GLU SER ALA ALA ALA ALA GLU          
SEQRES   8 C  503  ALA GLU SER TRP ASN SER VAL SER GLU GLY LYS GLN PRO          
SEQRES   9 C  503  ARG PHE SER HIS ARG ILE PRO LEU LEU ILE PHE ASP GLN          
SEQRES  10 C  503  ASP GLU LYS GLY LYS ALA ARG ASP PHE PHE THR GLY GLN          
SEQRES  11 C  503  GLN GLN GLN VAL GLY GLY SER ILE ILE HIS LYS ALA SER          
SEQRES  12 C  503  ASN VAL MET HIS ILE GLU SER LYS GLN VAL VAL GLY PHE          
SEQRES  13 C  503  GLN LEU CYS SER ASN ASP THR SER ASP CYS ALA THR TYR          
SEQRES  14 C  503  THR PHE SER SER GLY ILE ASN ALA ILE GLN GLU TRP TYR          
SEQRES  15 C  503  LYS LEU HIS TYR MET ASN ILE MET ALA GLN VAL PRO LEU          
SEQRES  16 C  503  GLU LYS LYS ILE ASN MET SER TYR SER ALA GLU GLU LEU          
SEQRES  17 C  503  LEU VAL THR CYS PHE PHE ASP GLY VAL SER CYS ASP ALA          
SEQRES  18 C  503  ARG ASN PHE THR LEU PHE HIS HIS PRO MET HIS GLY ASN          
SEQRES  19 C  503  CYS TYR THR PHE ASN ASN ARG GLU ASN GLU THR ILE LEU          
SEQRES  20 C  503  SER THR SER MET GLY GLY SER GLU TYR GLY LEU GLN VAL          
SEQRES  21 C  503  ILE LEU TYR ILE ASN GLU GLU GLU TYR ASN PRO PHE LEU          
SEQRES  22 C  503  VAL SER SER THR GLY ALA LYS VAL ILE ILE HIS ARG GLN          
SEQRES  23 C  503  ASP GLU TYR PRO PHE VAL GLU ASP VAL GLY THR GLU ILE          
SEQRES  24 C  503  GLU THR ALA MET VAL THR SER ILE GLY MET HIS LEU THR          
SEQRES  25 C  503  GLU SER PHE LYS LEU SER GLU PRO TYR SER GLN CYS THR          
SEQRES  26 C  503  GLU ASP GLY SER ASP VAL PRO ILE ARG ASN ILE TYR ASN          
SEQRES  27 C  503  ALA ALA TYR SER LEU GLN ILE CYS LEU HIS SER CYS PHE          
SEQRES  28 C  503  GLN THR LYS MET VAL GLU LYS CYS GLY CYS ALA GLN TYR          
SEQRES  29 C  503  SER GLN PRO LEU PRO PRO ALA ALA ASN TYR CYS ASN TYR          
SEQRES  30 C  503  GLN GLN HIS PRO ASN TRP MET TYR CYS TYR TYR GLN LEU          
SEQRES  31 C  503  HIS ARG ALA PHE VAL GLN GLU GLU LEU GLY CYS GLN SER          
SEQRES  32 C  503  VAL CYS LYS GLU ALA CYS SER PHE LYS GLU TRP THR LEU          
SEQRES  33 C  503  THR THR SER LEU ALA GLN TRP PRO SER VAL VAL SER GLU          
SEQRES  34 C  503  LYS TRP LEU LEU PRO VAL LEU THR TRP ASP GLN GLY ARG          
SEQRES  35 C  503  GLN VAL ASN LYS LYS LEU ASN LYS THR ASP LEU ALA LYS          
SEQRES  36 C  503  LEU LEU ILE PHE TYR LYS ASP LEU ASN GLN ARG SER ILE          
SEQRES  37 C  503  MET GLU SER PRO ALA ASN SER ILE UNK UNK UNK UNK UNK          
SEQRES  38 C  503  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  39 C  503  UNK UNK UNK UNK UNK UNK UNK UNK UNK                          
SEQRES   1 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 D  106  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 D  106  UNK UNK                                                      
SEQRES   1 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 E  121  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  10 E  121  UNK UNK UNK UNK                                              
SEQRES   1 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 F  115  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                  
SEQRES   1 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 G  112  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 G  112  UNK UNK UNK UNK UNK UNK UNK UNK                              
HELIX    1 AA1 UNK A   80  UNK A   85  1                                   6    
HELIX    2 AA2 UNK A   95  UNK A  106  1                                  12    
HELIX    3 AA3 ILE A  143  LEU A  161  1                                  19    
HELIX    4 AA4 SER A  243  LEU A  260  1                                  18    
HELIX    5 AA5 SER A  261  LEU A  263  5                                   3    
HELIX    6 AA6 ASP A  273  ASN A  277  5                                   5    
HELIX    7 AA7 GLN A  413  CYS A  429  1                                  17    
HELIX    8 AA8 SER A  452  SER A  465  1                                  14    
HELIX    9 AA9 GLY A  470  CYS A  475  1                                   6    
HELIX   10 AB1 THR A  497  ASN A  511  1                                  15    
HELIX   11 AB2 UNK A  548  UNK A  559  1                                  12    
HELIX   12 AB3 UNK A  560  UNK A  569  1                                  10    
HELIX   13 AB4 UNK B   49  LEU B   75  1                                  27    
HELIX   14 AB5 LYS B  104  ILE B  108  5                                   5    
HELIX   15 AB6 LEU B  112  ALA B  128  1                                  17    
HELIX   16 AB7 ASN B  141  ASN B  146  1                                   6    
HELIX   17 AB8 GLN B  213  VAL B  230  1                                  18    
HELIX   18 AB9 PRO B  231  MET B  238  1                                   8    
HELIX   19 AC1 PRO B  241  MET B  245  1                                   5    
HELIX   20 AC2 GLY B  302  TYR B  306  5                                   5    
HELIX   21 AC3 MET B  354  SER B  359  1                                   6    
HELIX   22 AC4 ILE B  383  CYS B  399  1                                  17    
HELIX   23 AC5 ASP B  422  MET B  432  1                                  11    
HELIX   24 AC6 SER B  433  CYS B  444  1                                  12    
HELIX   25 AC7 TRP B  470  SER B  476  1                                   7    
HELIX   26 AC8 UNK B  519  UNK B  541  1                                  23    
HELIX   27 AC9 UNK C   51  TYR C   79  1                                  29    
HELIX   28 AD1 LEU C  114  TYR C  129  1                                  16    
HELIX   29 AD2 SER C  221  MET C  238  1                                  18    
HELIX   30 AD3 PRO C  242  SER C  250  1                                   9    
HELIX   31 AD4 GLY C  301  TYR C  304  5                                   4    
HELIX   32 AD5 SER C  390  CYS C  407  1                                  18    
HELIX   33 AD6 ASN C  430  GLN C  444  1                                  15    
HELIX   34 AD7 GLY C  448  CYS C  453  1                                   6    
HELIX   35 AD8 TRP C  479  GLN C  488  1                                  10    
HELIX   36 AD9 ASN C  497  LEU C  501  5                                   5    
HELIX   37 AE1 UNK C  528  UNK C  541  1                                  14    
HELIX   38 AE2 UNK C  541  UNK C  551  1                                  11    
HELIX   39 AE3 UNK E   53  UNK E   56  5                                   4    
HELIX   40 AE4 UNK E   87  UNK E   91  5                                   5    
HELIX   41 AE5 UNK G   84  UNK G   88  5                                   5    
SHEET    1 AA1 4 VAL A 114  LEU A 120  0                                        
SHEET    2 AA1 4 LYS A 534  PRO A 540 -1  O  SER A 537   N  ASN A 117           
SHEET    3 AA1 4 VAL A 373  ASP A 385  1  N  ASP A 385   O  GLU A 538           
SHEET    4 AA1 4 SER A 480  SER A 487 -1  O  SER A 483   N  GLU A 382           
SHEET    1 AA2 5 ILE A 279  PHE A 284  0                                        
SHEET    2 AA2 5 LEU A 328  ARG A 333 -1  O  SER A 329   N  ARG A 283           
SHEET    3 AA2 5 VAL A 521  PHE A 528 -1  O  VAL A 524   N  LEU A 330           
SHEET    4 AA2 5 VAL A 373  ASP A 385  1  N  ILE A 377   O  ASN A 525           
SHEET    5 AA2 5 TYR A 490  ARG A 492 -1  O  SER A 491   N  GLU A 374           
SHEET    1 AA3 5 SER A 295  HIS A 296  0                                        
SHEET    2 AA3 5 CYS A 305  THR A 307 -1  O  THR A 307   N  SER A 295           
SHEET    3 AA3 5 VAL A 130  CYS A 133 -1  N  ILE A 132   O  TYR A 306           
SHEET    4 AA3 5 ALA A 349  VAL A 353 -1  O  MET A 352   N  THR A 131           
SHEET    5 AA3 5 PHE A 367  LEU A 369 -1  O  PHE A 367   N  VAL A 351           
SHEET    1 AA4 2 GLN A 227  LEU A 228  0                                        
SHEET    2 AA4 2 PHE A 237  TYR A 238 -1  O  PHE A 237   N  LEU A 228           
SHEET    1 AA5 2 CYS A 394  THR A 395  0                                        
SHEET    2 AA5 2 LYS A 477  PRO A 478  1  O  LYS A 477   N  THR A 395           
SHEET    1 AA6 4 VAL B  79  SER B  84  0                                        
SHEET    2 AA6 4 ILE B 492  ALA B 511 -1  O  SER B 510   N  SER B  80           
SHEET    3 AA6 4 THR B 340  GLN B 352  1  N  ILE B 344   O  ASN B 496           
SHEET    4 AA6 4 ASN B 449  GLN B 452 -1  O  ASP B 450   N  LEU B 351           
SHEET    1 AA7 5 ILE B 246  LEU B 250  0                                        
SHEET    2 AA7 5 LEU B 295  ASP B 300 -1  O  LYS B 296   N  LEU B 250           
SHEET    3 AA7 5 ILE B 492  ALA B 511 -1  O  VAL B 493   N  LEU B 299           
SHEET    4 AA7 5 THR B 340  GLN B 352  1  N  ILE B 344   O  ASN B 496           
SHEET    5 AA7 5 MET B 455  ASP B 461 -1  O  SER B 458   N  SER B 343           
SHEET    1 AA8 2 MET B  90  ASP B  91  0                                        
SHEET    2 AA8 2 PRO B 285  SER B 286 -1  O  SER B 286   N  MET B  90           
SHEET    1 AA9 5 THR B 262  TYR B 266  0                                        
SHEET    2 AA9 5 GLY B 270  ILE B 274 -1  O  CYS B 272   N  ILE B 264           
SHEET    3 AA9 5 ALA B  94  ASN B  99 -1  N  ILE B  97   O  TYR B 273           
SHEET    4 AA9 5 VAL B 316  HIS B 321 -1  O  ARG B 317   N  CYS B  98           
SHEET    5 AA9 5 ILE B 334  ALA B 336 -1  O  ALA B 336   N  VAL B 316           
SHEET    1 AB1 2 LEU B 150  ASP B 154  0                                        
SHEET    2 AB1 2 CYS B 189  MET B 193 -1  O  LYS B 190   N  ILE B 153           
SHEET    1 AB2 4 VAL C  81  HIS C  88  0                                        
SHEET    2 AB2 4 LYS C 503  PRO C 520 -1  O  MET C 517   N  SER C  84           
SHEET    3 AB2 4 VAL C 352  SER C 362  1  N  ILE C 355   O  LEU C 505           
SHEET    4 AB2 4 PHE C 459  TRP C 462 -1  O  GLU C 461   N  THR C 360           
SHEET    1 AB3 6 VAL C 265  SER C 266  0                                        
SHEET    2 AB3 6 THR C 259  PHE C 262 -1  N  PHE C 262   O  VAL C 265           
SHEET    3 AB3 6 LEU C 306  ILE C 309 -1  O  GLN C 307   N  PHE C 261           
SHEET    4 AB3 6 LYS C 503  PRO C 520 -1  O  LEU C 504   N  VAL C 308           
SHEET    5 AB3 6 VAL C 352  SER C 362  1  N  ILE C 355   O  LEU C 505           
SHEET    6 AB3 6 THR C 465  ALA C 469 -1  O  SER C 467   N  SER C 354           
SHEET    1 AB4 2 LEU C  92  ASP C  93  0                                        
SHEET    2 AB4 2 SER C 296  THR C 297 -1  O  THR C 297   N  LEU C  92           
SHEET    1 AB5 5 THR C 273  HIS C 277  0                                        
SHEET    2 AB5 5 GLY C 281  PHE C 286 -1  O  GLY C 281   N  HIS C 277           
SHEET    3 AB5 5 ALA C  96  CYS C 100 -1  N  VAL C  97   O  PHE C 286           
SHEET    4 AB5 5 LYS C 328  HIS C 332 -1  O  LYS C 328   N  CYS C 100           
SHEET    5 AB5 5 THR C 345  GLU C 346 -1  O  THR C 345   N  VAL C 329           
SHEET    1 AB6 3 LEU C 161  ILE C 162  0                                        
SHEET    2 AB6 3 VAL C 202  LEU C 206 -1  O  GLY C 203   N  LEU C 161           
SHEET    3 AB6 3 ALA C 215  PHE C 219 -1  O  ALA C 215   N  LEU C 206           
SHEET    1 AB7 3 UNK D  24  UNK D  26  0                                        
SHEET    2 AB7 3 UNK D  37  UNK D  45 -1  O  UNK D  44   N  UNK D  25           
SHEET    3 AB7 3 UNK D  90  UNK D  98 -1  O  UNK D  95   N  UNK D  39           
SHEET    1 AB8 2 UNK D  30  UNK D  33  0                                        
SHEET    2 AB8 2 UNK D 123  UNK D 126  1  O  UNK D 125   N  UNK D  31           
SHEET    1 AB9 5 UNK D  73  UNK D  74  0                                        
SHEET    2 AB9 5 UNK D  66  UNK D  69 -1  N  UNK D  69   O  UNK D  73           
SHEET    3 AB9 5 UNK D  54  UNK D  56 -1  N  UNK D  55   O  UNK D  68           
SHEET    4 AB9 5 UNK D 107  UNK D 110 -1  O  UNK D 109   N  UNK D  54           
SHEET    5 AB9 5 UNK D 117  UNK D 118 -1  O  UNK D 117   N  UNK D 110           
SHEET    1 AC1 4 UNK E   4  UNK E   7  0                                        
SHEET    2 AC1 4 UNK E  21  UNK E  24 -1  O  UNK E  21   N  UNK E   7           
SHEET    3 AC1 4 UNK E  78  UNK E  83 -1  O  UNK E  79   N  UNK E  22           
SHEET    4 AC1 4 UNK E  68  UNK E  73 -1  N  UNK E  69   O  UNK E  82           
SHEET    1 AC2 2 UNK E  11  UNK E  12  0                                        
SHEET    2 AC2 2 UNK E 119  UNK E 120  1  O  UNK E 119   N  UNK E  12           
SHEET    1 AC3 5 UNK E  58  UNK E  59  0                                        
SHEET    2 AC3 5 UNK E  47  UNK E  51 -1  N  UNK E  50   O  UNK E  59           
SHEET    3 AC3 5 UNK E  34  UNK E  39 -1  N  UNK E  34   O  UNK E  51           
SHEET    4 AC3 5 UNK E  93  UNK E  99 -1  O  UNK E  97   N  UNK E  35           
SHEET    5 AC3 5 UNK E 109  UNK E 112 -1  O  UNK E 110   N  UNK E  98           
SHEET    1 AC4 4 UNK F   3  UNK F   5  0                                        
SHEET    2 AC4 4 UNK F  22  UNK F  25 -1  O  UNK F  23   N  UNK F   5           
SHEET    3 AC4 4 UNK F  78  UNK F  80 -1  O  UNK F  79   N  UNK F  22           
SHEET    4 AC4 4 UNK F  71  UNK F  73 -1  N  UNK F  71   O  UNK F  80           
SHEET    1 AC5 2 UNK F  10  UNK F  11  0                                        
SHEET    2 AC5 2 UNK F 114  UNK F 115  1  O  UNK F 115   N  UNK F  10           
SHEET    1 AC6 4 UNK F  57  UNK F  60  0                                        
SHEET    2 AC6 4 UNK F  47  UNK F  52 -1  N  UNK F  52   O  UNK F  57           
SHEET    3 AC6 4 UNK F  33  UNK F  37 -1  N  UNK F  36   O  UNK F  48           
SHEET    4 AC6 4 UNK F  95  UNK F  99 -1  O  UNK F  95   N  UNK F  37           
SHEET    1 AC7 2 UNK G   4  UNK G   6  0                                        
SHEET    2 AC7 2 UNK G  23  UNK G  25 -1  O  UNK G  24   N  UNK G   5           
SHEET    1 AC8 4 UNK G  53  UNK G  54  0                                        
SHEET    2 AC8 4 UNK G  38  UNK G  43 -1  N  UNK G  40   O  UNK G  53           
SHEET    3 AC8 4 UNK G  90  UNK G  95 -1  O  UNK G  92   N  UNK G  41           
SHEET    4 AC8 4 UNK G 107  UNK G 108 -1  O  UNK G 107   N  UNK G  91           
SSBOND   1 CYS A  133    CYS A  305                          1555   1555  2.05  
SSBOND   2 CYS A  229    CYS A  236                          1555   1555  2.05  
SSBOND   3 CYS A  282    CYS A  289                          1555   1555  2.05  
SSBOND   4 CYS A  394    CYS A  479                          1555   1555  2.05  
SSBOND   5 CYS A  416    CYS A  475                          1555   1555  2.04  
SSBOND   6 CYS A  420    CYS A  471                          1555   1555  2.05  
SSBOND   7 CYS A  429    CYS A  456                          1555   1555  2.03  
SSBOND   8 CYS A  431    CYS A  445                          1555   1555  2.05  
SSBOND   9 CYS B   98    CYS B  272                          1555   1555  2.05  
SSBOND  10 CYS B  184    CYS B  189                          1555   1555  2.05  
SSBOND  11 CYS B  196    CYS B  203                          1555   1555  2.05  
SSBOND  12 CYS B  249    CYS B  256                          1555   1555  2.05  
SSBOND  13 CYS B  361    CYS B  448                          1555   1555  2.05  
SSBOND  14 CYS B  386    CYS B  444                          1555   1555  2.05  
SSBOND  15 CYS B  390    CYS B  440                          1555   1555  2.05  
SSBOND  16 CYS B  399    CYS B  426                          1555   1555  2.03  
SSBOND  17 CYS B  401    CYS B  415                          1555   1555  2.05  
SSBOND  18 CYS C  100    CYS C  283                          1555   1555  2.05  
SSBOND  19 CYS C  207    CYS C  214                          1555   1555  2.05  
SSBOND  20 CYS C  260    CYS C  267                          1555   1555  2.05  
SSBOND  21 CYS C  372    CYS C  457                          1555   1555  2.05  
SSBOND  22 CYS C  394    CYS C  453                          1555   1555  2.05  
SSBOND  23 CYS C  398    CYS C  449                          1555   1555  2.05  
SSBOND  24 CYS C  407    CYS C  434                          1555   1555  2.03  
SSBOND  25 CYS C  409    CYS C  423                          1555   1555  2.05  
LINK         NH2 ARG A 448                 O   UNK D  87     1555   1555  1.30  
LINK         CB  UNK C  63                 CB  UNK C 541     1555   1555  1.49  
LINK         CB  UNK C  67                 CB  UNK C 538     1555   1555  1.49  
LINK         CB  UNK C  70                 CB  UNK C 534     1555   1555  1.49  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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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