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Database: PDB
Entry: 5EK0
LinkDB: 5EK0
Original site: 5EK0 
HEADER    METAL TRANSPORT                         03-NOV-15   5EK0              
TITLE     HUMAN NAV1.7-VSD4-NAVAB IN COMPLEX WITH GX-936.                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA OF BACTERIAL ION TRANSPORT PROTEIN AND HUMAN SODIUM
COMPND   3 CHANNEL PROTEIN TYPE 9 SUBUNIT ALPHA;                                
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: EUROENDOCRINE SODIUM CHANNEL,HNE-NA,PERIPHERAL SODIUM       
COMPND   6 CHANNEL 1,PN1,SODIUM CHANNEL PROTEIN TYPE IX SUBUNIT ALPHA,VOLTAGE-  
COMPND   7 GATED SODIUM CHANNEL SUBUNIT ALPHA NAV1.7;                           
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCOBACTER BUTZLERI, HOMO SAPIENS;              
SOURCE   3 ORGANISM_TAXID: 367737, 9606;                                        
SOURCE   4 STRAIN: RM4018;                                                      
SOURCE   5 GENE: ABU_1752, SCN9A, NENA;                                         
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    MEMBRANE PROTEIN, ION CHANNEL, VOLTAGE-GATED SODIUM CHANNEL, SMALL    
KEYWDS   2 MOLECULE ANTAGONIST, METAL TRANSPORT                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.AHUJA,S.MUKUND,M.A.STAROVASNIK,C.M.KOTH,J.PAYANDEH                  
REVDAT   2   30-DEC-15 5EK0    1       JRNL                                     
REVDAT   1   23-DEC-15 5EK0    0                                                
JRNL        AUTH   S.AHUJA,S.MUKUND,L.DENG,K.KHAKH,E.CHANG,H.HO,S.SHRIVER,      
JRNL        AUTH 2 C.YOUNG,S.LIN,J.P.JOHNSON,P.WU,J.LI,M.COONS,C.TAM,           
JRNL        AUTH 3 B.BRILLANTES,H.SAMPANG,K.MORTARA,K.K.BOWMAN,K.R.CLARK,       
JRNL        AUTH 4 A.ESTEVEZ,Z.XIE,H.VERSCHOOF,M.GRIMWOOD,C.DEHNHARDT,          
JRNL        AUTH 5 J.C.ANDREZ,T.FOCKEN,D.P.SUTHERLIN,B.S.SAFINA,                
JRNL        AUTH 6 M.A.STAROVASNIK,D.F.ORTWINE,Y.FRANKE,C.J.COHEN,D.H.HACKOS,   
JRNL        AUTH 7 C.M.KOTH,J.PAYANDEH                                          
JRNL        TITL   STRUCTURAL BASIS OF NAV1.7 INHIBITION BY AN                  
JRNL        TITL 2 ISOFORM-SELECTIVE SMALL-MOLECULE ANTAGONIST.                 
JRNL        REF    SCIENCE                       V. 350 C5464 2015              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   26680203                                                     
JRNL        DOI    10.1126/SCIENCE.AAC5464                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33851                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.244                          
REMARK   3   R VALUE            (WORKING SET)  : 0.243                          
REMARK   3   FREE R VALUE                      : 0.272                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1714                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.53                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.64                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.73                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2845                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2479                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2697                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2473                   
REMARK   3   BIN FREE R VALUE                        : 0.2588                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.20                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 148                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8082                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 489                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 96.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 106.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -42.29980                                            
REMARK   3    B22 (A**2) : 47.93940                                             
REMARK   3    B33 (A**2) : -5.63960                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.871               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 2.842               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.466               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.836                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.821                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8780   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11913  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3036   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 120    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1211   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8780   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1150   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 11147  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.10                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.31                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.13                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215048.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3RVY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 AMMONIUM SULFATE, 100 MM SODIUM      
REMARK 280  CITRATE PH 5.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.56500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.56500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       84.71000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       94.41500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       84.71000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       94.41500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.56500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       84.71000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       94.41500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.56500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       84.71000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       94.41500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 27610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -231.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     MET A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     TYR A   -15                                                      
REMARK 465     LYS A   -14                                                      
REMARK 465     ASP A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     LYS A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     GLU A  1738                                                      
REMARK 465     VAL A  1739                                                      
REMARK 465     GLN A  1740                                                      
REMARK 465     SER A  1741                                                      
REMARK 465     HIS A  1742                                                      
REMARK 465     GLU A  1743                                                      
REMARK 465     ASP A  1744                                                      
REMARK 465     ASN A  1745                                                      
REMARK 465     ILE A  1746                                                      
REMARK 465     ASN A  1747                                                      
REMARK 465     ASN A  1748                                                      
REMARK 465     GLU A  1749                                                      
REMARK 465     ILE A  1750                                                      
REMARK 465     ILE A  1751                                                      
REMARK 465     LYS A  1752                                                      
REMARK 465     LEU A  1753                                                      
REMARK 465     ARG A  1754                                                      
REMARK 465     GLU A  1755                                                      
REMARK 465     GLU A  1756                                                      
REMARK 465     ILE A  1757                                                      
REMARK 465     VAL A  1758                                                      
REMARK 465     GLU A  1759                                                      
REMARK 465     LEU A  1760                                                      
REMARK 465     LYS A  1761                                                      
REMARK 465     GLU A  1762                                                      
REMARK 465     LEU A  1763                                                      
REMARK 465     ILE A  1764                                                      
REMARK 465     LYS A  1765                                                      
REMARK 465     THR A  1766                                                      
REMARK 465     SER A  1767                                                      
REMARK 465     LEU A  1768                                                      
REMARK 465     LYS A  1769                                                      
REMARK 465     ASN A  1770                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     ASP B   -16                                                      
REMARK 465     TYR B   -15                                                      
REMARK 465     LYS B   -14                                                      
REMARK 465     ASP B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     LYS B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLU B  1738                                                      
REMARK 465     VAL B  1739                                                      
REMARK 465     GLN B  1740                                                      
REMARK 465     SER B  1741                                                      
REMARK 465     HIS B  1742                                                      
REMARK 465     GLU B  1743                                                      
REMARK 465     ASP B  1744                                                      
REMARK 465     ASN B  1745                                                      
REMARK 465     ILE B  1746                                                      
REMARK 465     ASN B  1747                                                      
REMARK 465     ASN B  1748                                                      
REMARK 465     GLU B  1749                                                      
REMARK 465     ILE B  1750                                                      
REMARK 465     ILE B  1751                                                      
REMARK 465     LYS B  1752                                                      
REMARK 465     LEU B  1753                                                      
REMARK 465     ARG B  1754                                                      
REMARK 465     GLU B  1755                                                      
REMARK 465     GLU B  1756                                                      
REMARK 465     ILE B  1757                                                      
REMARK 465     VAL B  1758                                                      
REMARK 465     GLU B  1759                                                      
REMARK 465     LEU B  1760                                                      
REMARK 465     LYS B  1761                                                      
REMARK 465     GLU B  1762                                                      
REMARK 465     LEU B  1763                                                      
REMARK 465     ILE B  1764                                                      
REMARK 465     LYS B  1765                                                      
REMARK 465     THR B  1766                                                      
REMARK 465     SER B  1767                                                      
REMARK 465     LEU B  1768                                                      
REMARK 465     LYS B  1769                                                      
REMARK 465     ASN B  1770                                                      
REMARK 465     MET C   -17                                                      
REMARK 465     ASP C   -16                                                      
REMARK 465     TYR C   -15                                                      
REMARK 465     LYS C   -14                                                      
REMARK 465     ASP C   -13                                                      
REMARK 465     ASP C   -12                                                      
REMARK 465     ASP C   -11                                                      
REMARK 465     ASP C   -10                                                      
REMARK 465     LYS C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     PHE C  1592                                                      
REMARK 465     VAL C  1593                                                      
REMARK 465     SER C  1594                                                      
REMARK 465     GLU C  1738                                                      
REMARK 465     VAL C  1739                                                      
REMARK 465     GLN C  1740                                                      
REMARK 465     SER C  1741                                                      
REMARK 465     HIS C  1742                                                      
REMARK 465     GLU C  1743                                                      
REMARK 465     ASP C  1744                                                      
REMARK 465     ASN C  1745                                                      
REMARK 465     ILE C  1746                                                      
REMARK 465     ASN C  1747                                                      
REMARK 465     ASN C  1748                                                      
REMARK 465     GLU C  1749                                                      
REMARK 465     ILE C  1750                                                      
REMARK 465     ILE C  1751                                                      
REMARK 465     LYS C  1752                                                      
REMARK 465     LEU C  1753                                                      
REMARK 465     ARG C  1754                                                      
REMARK 465     GLU C  1755                                                      
REMARK 465     GLU C  1756                                                      
REMARK 465     ILE C  1757                                                      
REMARK 465     VAL C  1758                                                      
REMARK 465     GLU C  1759                                                      
REMARK 465     LEU C  1760                                                      
REMARK 465     LYS C  1761                                                      
REMARK 465     GLU C  1762                                                      
REMARK 465     LEU C  1763                                                      
REMARK 465     ILE C  1764                                                      
REMARK 465     LYS C  1765                                                      
REMARK 465     THR C  1766                                                      
REMARK 465     SER C  1767                                                      
REMARK 465     LEU C  1768                                                      
REMARK 465     LYS C  1769                                                      
REMARK 465     ASN C  1770                                                      
REMARK 465     MET D   -17                                                      
REMARK 465     ASP D   -16                                                      
REMARK 465     TYR D   -15                                                      
REMARK 465     LYS D   -14                                                      
REMARK 465     ASP D   -13                                                      
REMARK 465     ASP D   -12                                                      
REMARK 465     ASP D   -11                                                      
REMARK 465     ASP D   -10                                                      
REMARK 465     LYS D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     PHE D  1592                                                      
REMARK 465     VAL D  1593                                                      
REMARK 465     SER D  1594                                                      
REMARK 465     GLU D  1738                                                      
REMARK 465     VAL D  1739                                                      
REMARK 465     GLN D  1740                                                      
REMARK 465     SER D  1741                                                      
REMARK 465     HIS D  1742                                                      
REMARK 465     GLU D  1743                                                      
REMARK 465     ASP D  1744                                                      
REMARK 465     ASN D  1745                                                      
REMARK 465     ILE D  1746                                                      
REMARK 465     ASN D  1747                                                      
REMARK 465     ASN D  1748                                                      
REMARK 465     GLU D  1749                                                      
REMARK 465     ILE D  1750                                                      
REMARK 465     ILE D  1751                                                      
REMARK 465     LYS D  1752                                                      
REMARK 465     LEU D  1753                                                      
REMARK 465     ARG D  1754                                                      
REMARK 465     GLU D  1755                                                      
REMARK 465     GLU D  1756                                                      
REMARK 465     ILE D  1757                                                      
REMARK 465     VAL D  1758                                                      
REMARK 465     GLU D  1759                                                      
REMARK 465     LEU D  1760                                                      
REMARK 465     LYS D  1761                                                      
REMARK 465     GLU D  1762                                                      
REMARK 465     LEU D  1763                                                      
REMARK 465     ILE D  1764                                                      
REMARK 465     LYS D  1765                                                      
REMARK 465     THR D  1766                                                      
REMARK 465     SER D  1767                                                      
REMARK 465     LEU D  1768                                                      
REMARK 465     LYS D  1769                                                      
REMARK 465     ASN D  1770                                                      
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    GLU A1526      -43.74    -20.52                                   
REMARK 500    GLN A1528       99.28     92.73                                   
REMARK 500    ARG A1559     -126.57     55.11                                   
REMARK 500    PHE A1592       15.12    -53.21                                   
REMARK 500    SER A1594       87.98     72.55                                   
REMARK 500    GLN A1618      -32.45     82.86                                   
REMARK 500    LEU A1654      -78.35    -77.03                                   
REMARK 500    VAL A1693      -70.26    -74.69                                   
REMARK 500    TYR A1696       32.26    -98.69                                   
REMARK 500    TYR B1494        2.67     52.57                                   
REMARK 500    ILE B1500      -79.90    -71.05                                   
REMARK 500    GLU B1502       76.24     74.95                                   
REMARK 500    SER B1503     -136.19   -147.92                                   
REMARK 500    SER B1529      136.31     94.01                                   
REMARK 500    HIS B1558       69.50   -118.82                                   
REMARK 500    PHE B1592       86.17    -40.67                                   
REMARK 500    SER B1594      111.76     12.25                                   
REMARK 500    LEU B1603        0.48    -66.37                                   
REMARK 500    THR B1614      -82.20   -108.28                                   
REMARK 500    GLN B1618      -30.12     69.68                                   
REMARK 500    MET B1633        2.47   -160.09                                   
REMARK 500    LEU B1654      -70.08    -66.35                                   
REMARK 500    SER B1681       17.82     51.77                                   
REMARK 500    VAL C1523       43.21    -90.56                                   
REMARK 500    GLN C1528      -51.14   -122.17                                   
REMARK 500    SER C1529      122.15    147.90                                   
REMARK 500    ARG C1559      -86.94     51.90                                   
REMARK 500    ARG C1602       -8.49    -57.60                                   
REMARK 500    ARG C1611       -4.53    -58.10                                   
REMARK 500    THR C1614      -75.36    -86.25                                   
REMARK 500    GLN C1618      -52.48     77.80                                   
REMARK 500    LEU C1634      -28.84    -39.28                                   
REMARK 500    SER C1681       41.48     34.66                                   
REMARK 500    TYR C1696       53.22   -100.26                                   
REMARK 500    TYR D1494      -20.46   -156.32                                   
REMARK 500    VAL D1523       25.63    -72.33                                   
REMARK 500    SER D1529      124.06    109.71                                   
REMARK 500    VAL D1557      -42.25   -156.06                                   
REMARK 500    ARG D1559      -86.99     53.56                                   
REMARK 500    ARG D1602      -18.68    -47.27                                   
REMARK 500    GLN D1618      -35.90    175.04                                   
REMARK 500    GLU D1657      -71.46    -72.53                                   
REMARK 500    SER D1681       29.31     47.67                                   
REMARK 500    ILE D1686      -63.37   -124.61                                   
REMARK 500    ILE D1736      -62.89   -150.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PX4 A 1801                                                       
REMARK 610     PX4 A 1802                                                       
REMARK 610     PX4 A 1803                                                       
REMARK 610     PX4 A 1804                                                       
REMARK 610     PX4 A 1805                                                       
REMARK 610     PX4 A 1806                                                       
REMARK 610     PX4 A 1807                                                       
REMARK 610     PX4 B 1801                                                       
REMARK 610     PX4 B 1802                                                       
REMARK 610     PX4 B 1803                                                       
REMARK 610     PX4 B 1804                                                       
REMARK 610     PX4 B 1805                                                       
REMARK 610     PX4 C 1801                                                       
REMARK 610     PX4 C 1802                                                       
REMARK 610     PX4 C 1803                                                       
REMARK 610     PX4 C 1804                                                       
REMARK 610     PX4 D 1801                                                       
REMARK 610     PX4 D 1802                                                       
REMARK 610     PX4 D 1803                                                       
REMARK 610     PX4 D 1804                                                       
REMARK 610     PX4 D 1805                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 1807                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5P2 A 1808                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 B 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 B 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 B 1803                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 B 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 B 1805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5P2 B 1806                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 C 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 C 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 C 1803                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 C 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5P2 C 1805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 D 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 D 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 D 1805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5P2 D 1806                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT IS A CHIMERA BETWEEN THE BACTERIAL NAVAB CHANNEL      
REMARK 999 (A8EVM5) AND HUMAN NAV1.7 (Q1585-3).                                 
DBREF  5EK0 A 1493  1515  UNP    A8EVM5   A8EVM5_ARCB4     1     23             
DBREF  5EK0 A 1516  1548  UNP    Q15858   SCN9A_HUMAN   1527   1559             
DBREF  5EK0 A 1549  1569  UNP    A8EVM5   A8EVM5_ARCB4    58     78             
DBREF  5EK0 A 1570  1611  UNP    Q15858   SCN9A_HUMAN   1581   1622             
DBREF  5EK0 A 1612  1770  UNP    A8EVM5   A8EVM5_ARCB4   109    267             
DBREF  5EK0 B 1493  1515  UNP    A8EVM5   A8EVM5_ARCB4     1     23             
DBREF  5EK0 B 1516  1548  UNP    Q15858   SCN9A_HUMAN   1527   1559             
DBREF  5EK0 B 1549  1569  UNP    A8EVM5   A8EVM5_ARCB4    58     78             
DBREF  5EK0 B 1570  1611  UNP    Q15858   SCN9A_HUMAN   1581   1622             
DBREF  5EK0 B 1612  1770  UNP    A8EVM5   A8EVM5_ARCB4   109    267             
DBREF  5EK0 C 1493  1515  UNP    A8EVM5   A8EVM5_ARCB4     1     23             
DBREF  5EK0 C 1516  1548  UNP    Q15858   SCN9A_HUMAN   1527   1559             
DBREF  5EK0 C 1549  1569  UNP    A8EVM5   A8EVM5_ARCB4    58     78             
DBREF  5EK0 C 1570  1611  UNP    Q15858   SCN9A_HUMAN   1581   1622             
DBREF  5EK0 C 1612  1770  UNP    A8EVM5   A8EVM5_ARCB4   109    267             
DBREF  5EK0 D 1493  1515  UNP    A8EVM5   A8EVM5_ARCB4     1     23             
DBREF  5EK0 D 1516  1548  UNP    Q15858   SCN9A_HUMAN   1527   1559             
DBREF  5EK0 D 1549  1569  UNP    A8EVM5   A8EVM5_ARCB4    58     78             
DBREF  5EK0 D 1570  1611  UNP    Q15858   SCN9A_HUMAN   1581   1622             
DBREF  5EK0 D 1612  1770  UNP    A8EVM5   A8EVM5_ARCB4   109    267             
SEQADV 5EK0 MET A  -17  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 5EK0 ASP A  -16  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 TYR A  -15  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS A  -14  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP A  -13  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP A  -12  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP A  -11  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP A  -10  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS A   -9  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY A   -8  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER A   -7  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LEU A   -6  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 VAL A   -5  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 PRO A   -4  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ARG A   -3  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY A   -2  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER A   -1  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 HIS A    0  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 MET B  -17  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 5EK0 ASP B  -16  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 TYR B  -15  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS B  -14  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP B  -13  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP B  -12  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP B  -11  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP B  -10  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS B   -9  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY B   -8  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER B   -7  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LEU B   -6  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 VAL B   -5  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 PRO B   -4  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ARG B   -3  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY B   -2  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER B   -1  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 HIS B    0  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 MET C  -17  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 5EK0 ASP C  -16  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 TYR C  -15  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS C  -14  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP C  -13  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP C  -12  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP C  -11  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP C  -10  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS C   -9  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY C   -8  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER C   -7  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LEU C   -6  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 VAL C   -5  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 PRO C   -4  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ARG C   -3  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY C   -2  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER C   -1  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 HIS C    0  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 MET D  -17  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 5EK0 ASP D  -16  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 TYR D  -15  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS D  -14  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP D  -13  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP D  -12  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP D  -11  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ASP D  -10  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LYS D   -9  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY D   -8  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER D   -7  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 LEU D   -6  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 VAL D   -5  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 PRO D   -4  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 ARG D   -3  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 GLY D   -2  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 SER D   -1  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 5EK0 HIS D    0  UNP  A8EVM5              EXPRESSION TAG                 
SEQRES   1 A  296  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 A  296  PRO ARG GLY SER HIS MET TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 A  296  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 A  296  ILE VAL LEU ASN MET VAL THR MET MET VAL GLU LYS GLU          
SEQRES   5 A  296  GLY GLN SER GLN HIS MET THR GLU VAL LEU TYR TRP ILE          
SEQRES   6 A  296  ASN VAL VAL PHE ILE ILE LEU PHE THR ILE GLU ILE ILE          
SEQRES   7 A  296  LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS ASP          
SEQRES   8 A  296  PRO TRP SER LEU PHE ASP PHE VAL VAL VAL ILE ILE SER          
SEQRES   9 A  296  ILE VAL GLY MET PHE LEU ALA ASP LEU ILE GLU THR TYR          
SEQRES  10 A  296  PHE VAL SER PRO THR LEU PHE ARG VAL ILE ARG LEU ALA          
SEQRES  11 A  296  ARG ILE GLY ARG ILE LEU ARG LEU VAL THR ALA VAL PRO          
SEQRES  12 A  296  GLN MET ARG LYS ILE VAL SER ALA LEU ILE SER VAL ILE          
SEQRES  13 A  296  PRO GLY MET LEU SER VAL ILE ALA LEU MET THR LEU PHE          
SEQRES  14 A  296  PHE TYR ILE PHE ALA ILE MET ALA THR GLN LEU PHE GLY          
SEQRES  15 A  296  GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY GLU SER          
SEQRES  16 A  296  PHE TYR THR LEU PHE GLN VAL MET THR LEU GLU SER TRP          
SEQRES  17 A  296  SER MET GLY ILE VAL ARG PRO LEU MET GLU VAL TYR PRO          
SEQRES  18 A  296  TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE VAL VAL          
SEQRES  19 A  296  THR PHE VAL MET ILE ASN LEU VAL VAL ALA ILE ILE VAL          
SEQRES  20 A  296  ASP ALA MET ALA ILE LEU ASN GLN LYS GLU GLU GLN HIS          
SEQRES  21 A  296  ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN ILE ASN          
SEQRES  22 A  296  ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL GLU LEU          
SEQRES  23 A  296  LYS GLU LEU ILE LYS THR SER LEU LYS ASN                      
SEQRES   1 B  296  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 B  296  PRO ARG GLY SER HIS MET TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 B  296  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 B  296  ILE VAL LEU ASN MET VAL THR MET MET VAL GLU LYS GLU          
SEQRES   5 B  296  GLY GLN SER GLN HIS MET THR GLU VAL LEU TYR TRP ILE          
SEQRES   6 B  296  ASN VAL VAL PHE ILE ILE LEU PHE THR ILE GLU ILE ILE          
SEQRES   7 B  296  LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS ASP          
SEQRES   8 B  296  PRO TRP SER LEU PHE ASP PHE VAL VAL VAL ILE ILE SER          
SEQRES   9 B  296  ILE VAL GLY MET PHE LEU ALA ASP LEU ILE GLU THR TYR          
SEQRES  10 B  296  PHE VAL SER PRO THR LEU PHE ARG VAL ILE ARG LEU ALA          
SEQRES  11 B  296  ARG ILE GLY ARG ILE LEU ARG LEU VAL THR ALA VAL PRO          
SEQRES  12 B  296  GLN MET ARG LYS ILE VAL SER ALA LEU ILE SER VAL ILE          
SEQRES  13 B  296  PRO GLY MET LEU SER VAL ILE ALA LEU MET THR LEU PHE          
SEQRES  14 B  296  PHE TYR ILE PHE ALA ILE MET ALA THR GLN LEU PHE GLY          
SEQRES  15 B  296  GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY GLU SER          
SEQRES  16 B  296  PHE TYR THR LEU PHE GLN VAL MET THR LEU GLU SER TRP          
SEQRES  17 B  296  SER MET GLY ILE VAL ARG PRO LEU MET GLU VAL TYR PRO          
SEQRES  18 B  296  TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE VAL VAL          
SEQRES  19 B  296  THR PHE VAL MET ILE ASN LEU VAL VAL ALA ILE ILE VAL          
SEQRES  20 B  296  ASP ALA MET ALA ILE LEU ASN GLN LYS GLU GLU GLN HIS          
SEQRES  21 B  296  ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN ILE ASN          
SEQRES  22 B  296  ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL GLU LEU          
SEQRES  23 B  296  LYS GLU LEU ILE LYS THR SER LEU LYS ASN                      
SEQRES   1 C  296  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 C  296  PRO ARG GLY SER HIS MET TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 C  296  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 C  296  ILE VAL LEU ASN MET VAL THR MET MET VAL GLU LYS GLU          
SEQRES   5 C  296  GLY GLN SER GLN HIS MET THR GLU VAL LEU TYR TRP ILE          
SEQRES   6 C  296  ASN VAL VAL PHE ILE ILE LEU PHE THR ILE GLU ILE ILE          
SEQRES   7 C  296  LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS ASP          
SEQRES   8 C  296  PRO TRP SER LEU PHE ASP PHE VAL VAL VAL ILE ILE SER          
SEQRES   9 C  296  ILE VAL GLY MET PHE LEU ALA ASP LEU ILE GLU THR TYR          
SEQRES  10 C  296  PHE VAL SER PRO THR LEU PHE ARG VAL ILE ARG LEU ALA          
SEQRES  11 C  296  ARG ILE GLY ARG ILE LEU ARG LEU VAL THR ALA VAL PRO          
SEQRES  12 C  296  GLN MET ARG LYS ILE VAL SER ALA LEU ILE SER VAL ILE          
SEQRES  13 C  296  PRO GLY MET LEU SER VAL ILE ALA LEU MET THR LEU PHE          
SEQRES  14 C  296  PHE TYR ILE PHE ALA ILE MET ALA THR GLN LEU PHE GLY          
SEQRES  15 C  296  GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY GLU SER          
SEQRES  16 C  296  PHE TYR THR LEU PHE GLN VAL MET THR LEU GLU SER TRP          
SEQRES  17 C  296  SER MET GLY ILE VAL ARG PRO LEU MET GLU VAL TYR PRO          
SEQRES  18 C  296  TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE VAL VAL          
SEQRES  19 C  296  THR PHE VAL MET ILE ASN LEU VAL VAL ALA ILE ILE VAL          
SEQRES  20 C  296  ASP ALA MET ALA ILE LEU ASN GLN LYS GLU GLU GLN HIS          
SEQRES  21 C  296  ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN ILE ASN          
SEQRES  22 C  296  ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL GLU LEU          
SEQRES  23 C  296  LYS GLU LEU ILE LYS THR SER LEU LYS ASN                      
SEQRES   1 D  296  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 D  296  PRO ARG GLY SER HIS MET TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 D  296  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 D  296  ILE VAL LEU ASN MET VAL THR MET MET VAL GLU LYS GLU          
SEQRES   5 D  296  GLY GLN SER GLN HIS MET THR GLU VAL LEU TYR TRP ILE          
SEQRES   6 D  296  ASN VAL VAL PHE ILE ILE LEU PHE THR ILE GLU ILE ILE          
SEQRES   7 D  296  LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS ASP          
SEQRES   8 D  296  PRO TRP SER LEU PHE ASP PHE VAL VAL VAL ILE ILE SER          
SEQRES   9 D  296  ILE VAL GLY MET PHE LEU ALA ASP LEU ILE GLU THR TYR          
SEQRES  10 D  296  PHE VAL SER PRO THR LEU PHE ARG VAL ILE ARG LEU ALA          
SEQRES  11 D  296  ARG ILE GLY ARG ILE LEU ARG LEU VAL THR ALA VAL PRO          
SEQRES  12 D  296  GLN MET ARG LYS ILE VAL SER ALA LEU ILE SER VAL ILE          
SEQRES  13 D  296  PRO GLY MET LEU SER VAL ILE ALA LEU MET THR LEU PHE          
SEQRES  14 D  296  PHE TYR ILE PHE ALA ILE MET ALA THR GLN LEU PHE GLY          
SEQRES  15 D  296  GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY GLU SER          
SEQRES  16 D  296  PHE TYR THR LEU PHE GLN VAL MET THR LEU GLU SER TRP          
SEQRES  17 D  296  SER MET GLY ILE VAL ARG PRO LEU MET GLU VAL TYR PRO          
SEQRES  18 D  296  TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE VAL VAL          
SEQRES  19 D  296  THR PHE VAL MET ILE ASN LEU VAL VAL ALA ILE ILE VAL          
SEQRES  20 D  296  ASP ALA MET ALA ILE LEU ASN GLN LYS GLU GLU GLN HIS          
SEQRES  21 D  296  ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN ILE ASN          
SEQRES  22 D  296  ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL GLU LEU          
SEQRES  23 D  296  LYS GLU LEU ILE LYS THR SER LEU LYS ASN                      
HET    PX4  A1801      15                                                       
HET    PX4  A1802      31                                                       
HET    PX4  A1803       6                                                       
HET    PX4  A1804      11                                                       
HET    PX4  A1805       6                                                       
HET    PX4  A1806       7                                                       
HET    PX4  A1807      15                                                       
HET    5P2  A1808      39                                                       
HET    PX4  B1801      15                                                       
HET    PX4  B1802      31                                                       
HET    PX4  B1803      28                                                       
HET    PX4  B1804       6                                                       
HET    PX4  B1805      23                                                       
HET    5P2  B1806      39                                                       
HET    PX4  C1801      14                                                       
HET    PX4  C1802      34                                                       
HET    PX4  C1803       8                                                       
HET    PX4  C1804       9                                                       
HET    5P2  C1805      39                                                       
HET    PX4  D1801      28                                                       
HET    PX4  D1802      15                                                       
HET    PX4  D1803       5                                                       
HET    PX4  D1804       6                                                       
HET    PX4  D1805      20                                                       
HET    5P2  D1806      39                                                       
HETNAM     PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE                      
HETNAM     5P2 3-CYANO-4-[2-[2-(1-ETHYLAZETIDIN-3-YL)PYRAZOL-3-YL]-4-           
HETNAM   2 5P2  (TRIFLUOROMETHYL)PHENOXY]-~{N}-(1,2,4-THIADIAZOL-5-             
HETNAM   3 5P2  YL)BENZENESULFONAMIDE                                           
HETSYN     5P2 GX-936                                                           
FORMUL   5  PX4    21(C36 H73 N O8 P 1+)                                        
FORMUL  12  5P2    4(C24 H20 F3 N7 O3 S2)                                       
HELIX    1 AA1 HIS A    0  ARG A 1496  5                                   5    
HELIX    2 AA2 ILE A 1497  GLU A 1502  1                                   6    
HELIX    3 AA3 SER A 1503  VAL A 1523  1                                  21    
HELIX    4 AA4 SER A 1529  ARG A 1559  1                                  31    
HELIX    5 AA5 ARG A 1559  LYS A 1564  1                                   6    
HELIX    6 AA6 ASP A 1565  TYR A 1591  1                                  27    
HELIX    7 AA7 SER A 1594  ARG A 1602  1                                   9    
HELIX    8 AA8 ARG A 1605  ARG A 1611  1                                   7    
HELIX    9 AA9 ARG A 1611  VAL A 1616  1                                   6    
HELIX   10 AB1 GLN A 1618  SER A 1628  1                                  11    
HELIX   11 AB2 VAL A 1629  PHE A 1655  1                                  27    
HELIX   12 AB3 PHE A 1659  GLY A 1664  1                                   6    
HELIX   13 AB4 THR A 1665  THR A 1678  1                                  14    
HELIX   14 AB5 ILE A 1686  TYR A 1694  1                                   9    
HELIX   15 AB6 ALA A 1697  ASP A 1737  1                                  41    
HELIX   16 AB7 TYR B 1494  VAL B 1501  1                                   8    
HELIX   17 AB8 SER B 1504  MET B 1522  1                                  19    
HELIX   18 AB9 SER B 1529  HIS B 1558  1                                  30    
HELIX   19 AC1 ILE B 1560  ASP B 1565  1                                   6    
HELIX   20 AC2 ASP B 1565  TYR B 1591  1                                  27    
HELIX   21 AC3 SER B 1594  ARG B 1602  1                                   9    
HELIX   22 AC4 LEU B 1603  THR B 1614  5                                  12    
HELIX   23 AC5 GLN B 1618  SER B 1628  1                                  11    
HELIX   24 AC6 VAL B 1629  GLY B 1632  5                                   4    
HELIX   25 AC7 MET B 1633  PHE B 1655  1                                  23    
HELIX   26 AC8 PHE B 1659  GLY B 1664  1                                   6    
HELIX   27 AC9 THR B 1665  THR B 1678  1                                  14    
HELIX   28 AD1 ILE B 1686  TYR B 1694  1                                   9    
HELIX   29 AD2 ALA B 1697  ASP B 1737  1                                  41    
HELIX   30 AD3 TYR C 1494  GLU C 1502  1                                   9    
HELIX   31 AD4 SER C 1503  VAL C 1523  1                                  21    
HELIX   32 AD5 SER C 1529  ARG C 1559  1                                  31    
HELIX   33 AD6 ASP C 1565  TYR C 1591  1                                  27    
HELIX   34 AD7 THR C 1596  ARG C 1602  1                                   7    
HELIX   35 AD8 ARG C 1605  ALA C 1615  1                                  11    
HELIX   36 AD9 GLN C 1618  SER C 1628  1                                  11    
HELIX   37 AE1 VAL C 1629  PHE C 1655  1                                  27    
HELIX   38 AE2 PHE C 1659  GLY C 1664  1                                   6    
HELIX   39 AE3 THR C 1665  LEU C 1679  1                                  15    
HELIX   40 AE4 ILE C 1686  TYR C 1694  1                                   9    
HELIX   41 AE5 ALA C 1697  ASP C 1737  1                                  41    
HELIX   42 AE6 ARG D 1496  GLU D 1502  1                                   7    
HELIX   43 AE7 SER D 1503  VAL D 1523  1                                  21    
HELIX   44 AE8 SER D 1529  ARG D 1559  1                                  31    
HELIX   45 AE9 ILE D 1560  LYS D 1564  5                                   5    
HELIX   46 AF1 ASP D 1565  TYR D 1591  1                                  27    
HELIX   47 AF2 THR D 1596  LEU D 1603  1                                   8    
HELIX   48 AF3 ARG D 1605  VAL D 1616  1                                  12    
HELIX   49 AF4 GLN D 1618  SER D 1628  1                                  11    
HELIX   50 AF5 VAL D 1629  GLY D 1656  1                                  28    
HELIX   51 AF6 PHE D 1659  GLY D 1664  1                                   6    
HELIX   52 AF7 THR D 1665  THR D 1678  1                                  14    
HELIX   53 AF8 ILE D 1686  TYR D 1694  1                                   9    
HELIX   54 AF9 ALA D 1697  ILE D 1735  1                                  39    
CISPEP   1 ARG A   -3    GLY A   -2          0         3.85                     
CISPEP   2 GLY A 1527    GLN A 1528          0         4.06                     
CISPEP   3 GLY B 1527    GLN B 1528          0         0.81                     
CISPEP   4 GLY C 1527    GLN C 1528          0        -2.04                     
CISPEP   5 GLY D 1527    GLN D 1528          0        -0.80                     
SITE     1 AC1  6 LEU A1654  PHE A1655  TYR A1694  PRO A1695                    
SITE     2 AC1  6 TYR A1696  ARG D1599                                          
SITE     1 AC2  7 THR A1665  GLY A1667  GLU A1668  PHE A1670                    
SITE     2 AC2  7 TYR A1671  PRO B1695  TRP B1698                               
SITE     1 AC3  1 GLN A1618                                                     
SITE     1 AC4  3 GLN A1530  GLU A1534  5P2 A1808                               
SITE     1 AC5 16 GLU A1534  TYR A1537  TRP A1538  ASN A1540                    
SITE     2 AC5 16 VAL A1541  GLY A1581  MET A1582  PHE A1583                    
SITE     3 AC5 16 ALA A1585  ASP A1586  PHE A1598  ARG A1602                    
SITE     4 AC5 16 ALA A1604  ARG A1605  ARG A1608  PX4 A1807                    
SITE     1 AC6  6 THR A1596  ARG A1599  TYR B1694  PRO B1695                    
SITE     2 AC6  6 TYR B1696  ALA B1697                                          
SITE     1 AC7  8 THR B1665  GLY B1667  GLU B1668  PHE B1670                    
SITE     2 AC7  8 TYR B1671  MET C1691  PRO C1695  TRP C1698                    
SITE     1 AC8  1 GLN B1618                                                     
SITE     1 AC9  1 MET B1677                                                     
SITE     1 AD1  3 GLU B1534  ASP B1586  5P2 B1806                               
SITE     1 AD2 15 GLU B1534  TYR B1537  TRP B1538  ASN B1540                    
SITE     2 AD2 15 VAL B1541  GLY B1581  MET B1582  PHE B1583                    
SITE     3 AD2 15 ALA B1585  ASP B1586  PHE B1598  ARG B1602                    
SITE     4 AD2 15 ARG B1605  ARG B1608  PX4 B1805                               
SITE     1 AD3  4 THR B1596  TYR C1694  PRO C1695  TYR C1696                    
SITE     1 AD4  7 TYR C1645  THR C1665  GLY C1667  GLU C1668                    
SITE     2 AD4  7 PHE C1670  TYR D1696  TRP D1698                               
SITE     1 AD5  1 GLN C1618                                                     
SITE     1 AD6  3 GLU C1534  TRP C1538  5P2 C1805                               
SITE     1 AD7 16 TYR C1537  TRP C1538  ASN C1540  GLY C1581                    
SITE     2 AD7 16 MET C1582  PHE C1583  ALA C1585  ASP C1586                    
SITE     3 AD7 16 GLU C1589  THR C1590  PHE C1598  ARG C1602                    
SITE     4 AD7 16 ALA C1604  ARG C1605  ARG C1608  PX4 C1804                    
SITE     1 AD8  6 MET A1691  TRP A1698  PHE D1644  GLY D1667                    
SITE     2 AD8  6 GLU D1668  PHE D1670                                          
SITE     1 AD9  5 ARG C1599  PHE D1655  TYR D1694  PRO D1695                    
SITE     2 AD9  5 TYR D1696                                                     
SITE     1 AE1  2 GLU D1534  5P2 D1806                                          
SITE     1 AE2 17 GLU D1534  TYR D1537  TRP D1538  ASN D1540                    
SITE     2 AE2 17 VAL D1541  SER D1578  GLY D1581  MET D1582                    
SITE     3 AE2 17 PHE D1583  ALA D1585  ASP D1586  PHE D1598                    
SITE     4 AE2 17 ARG D1602  ALA D1604  ARG D1605  ARG D1608                    
SITE     5 AE2 17 PX4 D1805                                                     
CRYST1  169.420  188.830  171.130  90.00  90.00  90.00 C 2 2 21     32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005902  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005296  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005844        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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