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Database: PDB
Entry: 6RV3
LinkDB: 6RV3
Original site: 6RV3 
HEADER    MEMBRANE PROTEIN                        30-MAY-19   6RV3              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN TWO PORE DOMAIN POTASSIUM ION CHANNEL  
TITLE    2 TASK-1 (K2P3.1) IN A CLOSED CONFORMATION WITH A BOUND INHIBITOR BAY  
TITLE    3 1000493                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM CHANNEL SUBFAMILY K MEMBER 3;                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ACID-SENSITIVE POTASSIUM CHANNEL PROTEIN TASK-1,TWIK-RELATED
COMPND   5 ACID-SENSITIVE K(+) CHANNEL 1,TWO PORE POTASSIUM CHANNEL KT3.1,TWO   
COMPND   6 PORE K(+) CHANNEL KT3.1;                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: TWO-PORE DOMAIN POTASSIUM CHANNEL K2P3.1 (TASK-1)     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KCNK3, TASK, TASK1;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    MEMBRANE PROTEIN, POTASSIUM CHANNEL, STRUCTURAL GENOMICS, STRUCTURAL  
KEYWDS   2 GENOMICS CONSORTIUM, SGC                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.E.J.RODSTROM,A.C.W.PIKE,W.ZHANG,A.QUIGLEY,D.SPEEDMAN,               
AUTHOR   2 S.M.M.MUKHOPADHYAY,L.SHRESTHA,R.CHALK,S.VENKAYA,S.R.BUSHELL,         
AUTHOR   3 A.TESSITORE,N.BURGESS-BROWN,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,    
AUTHOR   4 E.P.CARPENTER,STRUCTURAL GENOMICS CONSORTIUM (SGC)                   
REVDAT   2   22-JUL-20 6RV3    1       JRNL                                     
REVDAT   1   07-AUG-19 6RV3    0                                                
JRNL        AUTH   K.E.J.RODSTROM,A.K.KIPER,W.ZHANG,S.RINNE,A.C.W.PIKE,         
JRNL        AUTH 2 M.GOLDSTEIN,L.J.CONRAD,M.DELBECK,M.G.HAHN,H.MEIER,M.PLATZK,  
JRNL        AUTH 3 A.QUIGLEY,D.SPEEDMAN,L.SHRESTHA,S.M.M.MUKHOPADHYAY,          
JRNL        AUTH 4 N.A.BURGESS-BROWN,S.J.TUCKER,T.MULLER,N.DECHER,E.P.CARPENTER 
JRNL        TITL   A LOWER X-GATE IN TASK CHANNELS TRAPS INHIBITORS WITHIN THE  
JRNL        TITL 2 VESTIBULE.                                                   
JRNL        REF    NATURE                        V. 582   443 2020              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   32499642                                                     
JRNL        DOI    10.1038/S41586-020-2250-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40419                          
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)  : 0.235                          
REMARK   3   R VALUE            (WORKING SET)  : 0.235                          
REMARK   3   FREE R VALUE                      : 0.242                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.770                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1926                           
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               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.94                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 37.87                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 809                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2391                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 776                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2393                   
REMARK   3   BIN FREE R VALUE                        : 0.2348                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.08                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
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            : 8070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 475                                     
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.99390                                            
REMARK   3    B22 (A**2) : 10.05590                                             
REMARK   3    B33 (A**2) : 1.93800                                              
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) : 0.470               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.851               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.341               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.888               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.348               
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      : 0.842                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8816   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11979  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3136   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 1436   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8816   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 10     ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1165   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : 64     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10311  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.92                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.07                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.41                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|1 - 304}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):    2.6233  -41.1758   26.2636           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3824 T22:   -0.0380                                    
REMARK   3     T33:   -0.2099 T12:    0.0044                                    
REMARK   3     T13:    0.0262 T23:    0.1777                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2514 L22:    1.0340                                    
REMARK   3     L33:    1.8772 L12:   -0.1789                                    
REMARK   3     L13:    0.5113 L23:   -0.1073                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0521 S12:    0.1621 S13:   -0.1800                     
REMARK   3     S21:   -0.1277 S22:   -0.0568 S23:    0.0306                     
REMARK   3     S31:    0.0726 S32:    0.1573 S33:    0.0047                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|1 - 261}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.7046  -37.3554   29.6618           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3452 T22:   -0.0777                                    
REMARK   3     T33:   -0.1404 T12:    0.0032                                    
REMARK   3     T13:   -0.0276 T23:    0.1633                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4477 L22:    0.7406                                    
REMARK   3     L33:    1.4522 L12:    0.3481                                    
REMARK   3     L13:    0.0652 L23:   -0.5113                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0411 S12:   -0.0652 S13:    0.1046                     
REMARK   3     S21:    0.0076 S22:   -0.0612 S23:    0.1536                     
REMARK   3     S31:   -0.0642 S32:   -0.2090 S33:    0.0201                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|1 - 304}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.2124   22.9701   33.1839           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3788 T22:   -0.0171                                    
REMARK   3     T33:   -0.1723 T12:    0.0396                                    
REMARK   3     T13:    0.0174 T23:   -0.0246                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9338 L22:    1.8049                                    
REMARK   3     L33:    1.3224 L12:    0.2038                                    
REMARK   3     L13:    0.0918 L23:   -0.2483                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0259 S12:    0.0724 S13:    0.1605                     
REMARK   3     S21:   -0.1742 S22:   -0.0804 S23:    0.0516                     
REMARK   3     S31:   -0.0392 S32:   -0.1788 S33:    0.1063                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {D|1 - 258}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.4208   18.7541   36.7242           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3880 T22:   -0.0467                                    
REMARK   3     T33:   -0.2089 T12:   -0.0154                                    
REMARK   3     T13:    0.0087 T23:   -0.0050                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7647 L22:    1.4857                                    
REMARK   3     L33:    1.6470 L12:    0.2180                                    
REMARK   3     L13:    0.0375 L23:    0.2597                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0534 S12:   -0.0376 S13:   -0.0699                     
REMARK   3     S21:   -0.1060 S22:    0.0639 S23:   -0.0863                     
REMARK   3     S31:    0.0954 S32:    0.1728 S33:   -0.0105                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINED AGAINST STARANISO                 
REMARK   3  ANISOTROPICALLY TRUNCATED DATA                                      
REMARK   4                                                                      
REMARK   4 6RV3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102625.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018           
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION JAN 26, 2018,       
REMARK 200                                   STARANISO 2.2.12                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40478                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.291                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.16800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.7.17                                         
REMARK 200 STARTING MODEL: 4BW5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.05 M KCL, 24% V/V   
REMARK 280  PEG 400, 3% W/V SUCROSE, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      119.66000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      119.66000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ARG A   151                                                      
REMARK 465     TYR A   262                                                      
REMARK 465     PHE A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     ARG B   150                                                      
REMARK 465     ARG B   151                                                      
REMARK 465     TYR B   262                                                      
REMARK 465     PHE B   263                                                      
REMARK 465     GLN B   264                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     ASN C   260                                                      
REMARK 465     LEU C   261                                                      
REMARK 465     TYR C   262                                                      
REMARK 465     PHE C   263                                                      
REMARK 465     GLN C   264                                                      
REMARK 465     TYR D   262                                                      
REMARK 465     PHE D   263                                                      
REMARK 465     GLN D   264                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   2    CE   NZ                                             
REMARK 470     GLU A  37    OE1  OE2                                            
REMARK 470     ASN A  53    CG   OD1  ND2                                       
REMARK 470     GLN A  56    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CD   CE   NZ                                        
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     ARG A  79    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 145    CE   NZ                                             
REMARK 470     LEU A 147    CG   CD1  CD2                                       
REMARK 470     LYS A 210    NZ                                                  
REMARK 470     LYS A 255    CE   NZ                                             
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 260    CG   OD1  ND2                                       
REMARK 470     LEU A 261    CG   CD1  CD2                                       
REMARK 470     LYS B   2    CD   CE   NZ                                        
REMARK 470     GLN B  56    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  62    CG   CD1  CD2                                       
REMARK 470     LYS B  70    CE   NZ                                             
REMARK 470     LYS B  73    CG   CD   CE   NZ                                   
REMARK 470     LYS B 145    CE   NZ                                             
REMARK 470     MET B 149    CG   SD   CE                                        
REMARK 470     ARG B 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 255    CG   CD   CE   NZ                                   
REMARK 470     ARG B 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 261    CG   CD1  CD2                                       
REMARK 470     LYS C   2    CD   CE   NZ                                        
REMARK 470     ARG C  38    CZ   NH1  NH2                                       
REMARK 470     ASN C  53    CG   OD1  ND2                                       
REMARK 470     GLN C  56    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  60    CD   OE1  OE2                                       
REMARK 470     GLU C  61    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  62    CG   CD1  CD2                                       
REMARK 470     ARG C  64    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C  70    CE   NZ                                             
REMARK 470     LYS C  73    CG   CD   CE   NZ                                   
REMARK 470     LYS C 145    CE   NZ                                             
REMARK 470     LEU C 147    CG   CD1  CD2                                       
REMARK 470     ARG C 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 255    CE   NZ                                             
REMARK 470     ARG C 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  48    CG   CD1  CD2                                       
REMARK 470     ARG D  51    NE   CZ   NH1  NH2                                  
REMARK 470     GLN D  56    CD   OE1  NE2                                       
REMARK 470     ARG D  68    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D  70    CG   CD   CE   NZ                                   
REMARK 470     LYS D  73    CG   CD   CE   NZ                                   
REMARK 470     LYS D 145    CD   CE   NZ                                        
REMARK 470     ARG D 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 153    CG   OD1  OD2                                       
REMARK 470     HIS D 183    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 210    CE   NZ                                             
REMARK 470     LYS D 255    CG   CD   CE   NZ                                   
REMARK 470     ARG D 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 261    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  79     -168.06    -76.16                                   
REMARK 500    GLN A 217       77.21   -116.78                                   
REMARK 500    ARG B  79     -166.40    -76.89                                   
REMARK 500    GLN B 217       76.90   -116.60                                   
REMARK 500    ARG C  79     -167.35    -77.26                                   
REMARK 500    GLN C 217       76.34   -116.70                                   
REMARK 500    ARG D  79     -165.75    -75.45                                   
REMARK 500    MET D 149      134.18   -170.24                                   
REMARK 500    ARG D 151       70.09   -101.81                                   
REMARK 500    GLN D 217       76.20   -116.23                                   
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     DMU A  307                                                       
REMARK 610     PC1 A  308                                                       
REMARK 610     DMU B  304                                                       
REMARK 610     DMU C  307                                                       
REMARK 610     PC1 D  701                                                       
REMARK 610     DMU D  704                                                       
REMARK 610     PC1 D  705                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 304   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  93   O                                                      
REMARK 620 2 THR A  93   OG1  67.2                                              
REMARK 620 3 THR A 199   O    66.0 108.7                                        
REMARK 620 4 THR A 199   OG1 103.8  75.8  67.2                                  
REMARK 620 5 THR B  93   O    98.2 165.2  64.8 111.3                            
REMARK 620 6 THR B  93   OG1 165.6 126.8 108.0  84.6  67.6                      
REMARK 620 7 THR B 199   O    62.9 104.1  98.7 164.4  65.4 106.8                
REMARK 620 8 THR B 199   OG1 107.6  81.8 162.4 130.1 101.5  74.1  64.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  93   O                                                      
REMARK 620 2 ILE A  94   O    74.7                                              
REMARK 620 3 THR A 199   O    70.5  88.3                                        
REMARK 620 4 ILE A 200   O   137.0  77.5  76.6                                  
REMARK 620 5 THR B  93   O   106.2 154.3  68.6  86.0                            
REMARK 620 6 ILE B  94   O   148.3 119.1 133.8  74.6  74.0                      
REMARK 620 7 THR B 199   O    66.5 131.0 105.0 151.2  68.6  85.1                
REMARK 620 8 ILE B 200   O    83.0  73.6 151.2 119.4 132.0  75.0  73.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A  94   O                                                      
REMARK 620 2 GLY A  95   O    71.0                                              
REMARK 620 3 ILE A 200   O    79.2 140.4                                        
REMARK 620 4 GLY A 201   O    81.4  76.8  73.5                                  
REMARK 620 5 ILE B  94   O   122.4 142.6  75.8 136.1                            
REMARK 620 6 GLY B  95   O   148.3 117.9  76.7  72.2  70.7                      
REMARK 620 7 ILE B 200   O    74.9  74.7 122.1 147.6  76.2 136.0                
REMARK 620 8 GLY B 201   O   132.9  69.8 147.1 113.4  78.7  75.4  70.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 309   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  95   O                                                      
REMARK 620 2 TYR A  96   O    75.2                                              
REMARK 620 3 GLY A 201   O    72.6  90.7                                        
REMARK 620 4 PHE A 202   O   132.9  72.9  74.2                                  
REMARK 620 5 GLY B  95   O   108.6 154.3  67.4  87.7                            
REMARK 620 6 TYR B  96   O   154.9 113.6 128.5  71.3  74.2                      
REMARK 620 7 GLY B 201   O    67.7 130.0 108.0 156.2  72.1  90.5                
REMARK 620 8 PHE B 202   O    88.4  72.0 157.3 112.9 132.5  73.3  74.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  93   O                                                      
REMARK 620 2 ILE C  94   O    75.5                                              
REMARK 620 3 THR C 199   O    71.2  89.5                                        
REMARK 620 4 ILE C 200   O   139.1  78.5  77.5                                  
REMARK 620 5 THR D  93   O   107.1 156.0  69.7  85.3                            
REMARK 620 6 ILE D  94   O   146.0 119.3 134.1  74.8  72.2                      
REMARK 620 7 THR D 199   O    66.9 131.6 105.3 149.2  67.9  82.6                
REMARK 620 8 ILE D 200   O    83.1  74.7 152.6 119.5 129.1  73.2  71.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 304   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  93   O                                                      
REMARK 620 2 THR C  93   OG1  68.2                                              
REMARK 620 3 THR C 199   O    66.3 108.9                                        
REMARK 620 4 THR C 199   OG1 103.9  75.8  66.0                                  
REMARK 620 5 THR D  93   O    98.6 166.8  64.4 109.4                            
REMARK 620 6 THR D  93   OG1 164.6 127.1 105.8  83.5  66.0                      
REMARK 620 7 THR D 199   O    64.4 106.9  99.2 164.6  64.8 105.5                
REMARK 620 8 THR D 199   OG1 109.5  83.6 162.6 130.3 100.8  73.8  64.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE C  94   O                                                      
REMARK 620 2 GLY C  95   O    70.9                                              
REMARK 620 3 ILE C 200   O    78.9 140.3                                        
REMARK 620 4 GLY C 201   O    81.0  76.5  73.9                                  
REMARK 620 5 ILE D  94   O   122.9 142.2  76.3 136.7                            
REMARK 620 6 GLY D  95   O   148.7 118.3  77.2  73.2  70.0                      
REMARK 620 7 ILE D 200   O    75.7  75.1 121.7 147.9  75.3 134.6                
REMARK 620 8 GLY D 201   O   133.2  70.5 146.8 114.1  77.4  74.9  69.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C  95   O                                                      
REMARK 620 2 TYR C  96   O    75.7                                              
REMARK 620 3 GLY C 201   O    72.2  90.9                                        
REMARK 620 4 PHE C 202   O   133.2  73.3  74.2                                  
REMARK 620 5 GLY D  95   O   107.8 155.1  67.8  88.0                            
REMARK 620 6 TYR D  96   O   154.2 114.0 128.9  72.0  74.0                      
REMARK 620 7 GLY D 201   O    68.2 130.5 108.2 155.2  71.0  89.1                
REMARK 620 8 PHE D 202   O    89.2  72.9 158.1 113.4 130.9  72.2  74.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 303                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 304                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 309                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KKQ A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 303                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 304                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KKQ C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU C 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU D 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 D 705                 
DBREF  6RV3 A    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV3 B    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV3 C    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV3 D    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
SEQADV 6RV3 ASN A  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 LEU A  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 TYR A  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 PHE A  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 GLN A  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 ASN B  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 LEU B  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 TYR B  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 PHE B  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 GLN B  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 ASN C  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 LEU C  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 TYR C  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 PHE C  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 GLN C  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 ASN D  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 LEU D  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 TYR D  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 PHE D  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV3 GLN D  264  UNP  O14649              EXPRESSION TAG                 
SEQRES   1 A  264  MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL          
SEQRES   2 A  264  CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE          
SEQRES   3 A  264  ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN          
SEQRES   4 A  264  ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR          
SEQRES   5 A  264  ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL          
SEQRES   6 A  264  VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP          
SEQRES   7 A  264  ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE          
SEQRES   8 A  264  THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP          
SEQRES   9 A  264  GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY          
SEQRES  10 A  264  ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU          
SEQRES  11 A  264  ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA          
SEQRES  12 A  264  LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET          
SEQRES  13 A  264  ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER          
SEQRES  14 A  264  THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU          
SEQRES  15 A  264  HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE          
SEQRES  16 A  264  THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU          
SEQRES  17 A  264  GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL          
SEQRES  18 A  264  ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL          
SEQRES  19 A  264  ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET          
SEQRES  20 A  264  THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN          
SEQRES  21 A  264  LEU TYR PHE GLN                                              
SEQRES   1 B  264  MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL          
SEQRES   2 B  264  CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE          
SEQRES   3 B  264  ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN          
SEQRES   4 B  264  ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR          
SEQRES   5 B  264  ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL          
SEQRES   6 B  264  VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP          
SEQRES   7 B  264  ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE          
SEQRES   8 B  264  THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP          
SEQRES   9 B  264  GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY          
SEQRES  10 B  264  ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU          
SEQRES  11 B  264  ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA          
SEQRES  12 B  264  LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET          
SEQRES  13 B  264  ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER          
SEQRES  14 B  264  THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU          
SEQRES  15 B  264  HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE          
SEQRES  16 B  264  THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU          
SEQRES  17 B  264  GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL          
SEQRES  18 B  264  ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL          
SEQRES  19 B  264  ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET          
SEQRES  20 B  264  THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN          
SEQRES  21 B  264  LEU TYR PHE GLN                                              
SEQRES   1 C  264  MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL          
SEQRES   2 C  264  CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE          
SEQRES   3 C  264  ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN          
SEQRES   4 C  264  ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR          
SEQRES   5 C  264  ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL          
SEQRES   6 C  264  VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP          
SEQRES   7 C  264  ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE          
SEQRES   8 C  264  THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP          
SEQRES   9 C  264  GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY          
SEQRES  10 C  264  ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU          
SEQRES  11 C  264  ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA          
SEQRES  12 C  264  LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET          
SEQRES  13 C  264  ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER          
SEQRES  14 C  264  THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU          
SEQRES  15 C  264  HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE          
SEQRES  16 C  264  THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU          
SEQRES  17 C  264  GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL          
SEQRES  18 C  264  ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL          
SEQRES  19 C  264  ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET          
SEQRES  20 C  264  THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN          
SEQRES  21 C  264  LEU TYR PHE GLN                                              
SEQRES   1 D  264  MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL          
SEQRES   2 D  264  CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE          
SEQRES   3 D  264  ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN          
SEQRES   4 D  264  ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR          
SEQRES   5 D  264  ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL          
SEQRES   6 D  264  VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP          
SEQRES   7 D  264  ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE          
SEQRES   8 D  264  THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP          
SEQRES   9 D  264  GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY          
SEQRES  10 D  264  ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU          
SEQRES  11 D  264  ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA          
SEQRES  12 D  264  LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET          
SEQRES  13 D  264  ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER          
SEQRES  14 D  264  THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU          
SEQRES  15 D  264  HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE          
SEQRES  16 D  264  THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU          
SEQRES  17 D  264  GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL          
SEQRES  18 D  264  ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL          
SEQRES  19 D  264  ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET          
SEQRES  20 D  264  THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN          
SEQRES  21 D  264  LEU TYR PHE GLN                                              
HET      K  A 301       1                                                       
HET      K  A 303       1                                                       
HET      K  A 304       1                                                       
HET    Y01  A 305      35                                                       
HET    Y01  A 306      35                                                       
HET    DMU  A 307      20                                                       
HET    PC1  A 308      16                                                       
HET      K  A 309       1                                                       
HET    KKQ  A 300      64                                                       
HET    Y01  B 302      35                                                       
HET    Y01  B 303      35                                                       
HET    DMU  B 304      20                                                       
HET      K  C 301       1                                                       
HET      K  C 302       1                                                       
HET      K  C 303       1                                                       
HET      K  C 304       1                                                       
HET    Y01  C 305      35                                                       
HET    KKQ  C 306      64                                                       
HET    DMU  C 307      22                                                       
HET    PC1  D 701      38                                                       
HET    Y01  D 702      35                                                       
HET    Y01  D 703      35                                                       
HET    DMU  D 704      22                                                       
HET    PC1  D 705      20                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     Y01 CHOLESTEROL HEMISUCCINATE                                        
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE                                     
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETNAM     KKQ [4-[[2-(4-BROMOPHENYL)IMIDAZO[1,2-A]PYRIDIN-3-                   
HETNAM   2 KKQ  YL]METHYL]PIPERAZIN-1-YL]-(2-FLUOROPHENYL)METHANONE             
HETSYN     DMU DECYLMALTOSIDE                                                   
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   5    K    8(K 1+)                                                      
FORMUL   8  Y01    7(C31 H50 O4)                                                
FORMUL  10  DMU    4(C22 H42 O11)                                               
FORMUL  11  PC1    3(C44 H88 N O8 P)                                            
FORMUL  13  KKQ    2(C25 H22 BR F N4 O)                                         
FORMUL  29  HOH   *31(H2 O)                                                     
HELIX    1 AA1 LYS A    2  TYR A   52  1                                  51    
HELIX    2 AA2 SER A   55  ALA A   74  1                                  20    
HELIX    3 AA3 ARG A   79  THR A   92  1                                  14    
HELIX    4 AA4 THR A  103  GLY A  148  1                                  46    
HELIX    5 AA5 SER A  155  GLU A  182  1                                  28    
HELIX    6 AA6 THR A  185  THR A  198  1                                  14    
HELIX    7 AA7 GLN A  212  GLN A  217  1                                   6    
HELIX    8 AA8 GLN A  217  VAL A  242  1                                  26    
HELIX    9 AA9 VAL A  243  THR A  248  1                                   6    
HELIX   10 AB1 THR A  248  LEU A  261  1                                  14    
HELIX   11 AB2 LYS B    2  TYR B   52  1                                  51    
HELIX   12 AB3 SER B   55  ALA B   74  1                                  20    
HELIX   13 AB4 ARG B   79  THR B   92  1                                  14    
HELIX   14 AB5 THR B  103  GLY B  148  1                                  46    
HELIX   15 AB6 SER B  155  GLU B  182  1                                  28    
HELIX   16 AB7 THR B  185  THR B  198  1                                  14    
HELIX   17 AB8 GLN B  212  GLN B  217  1                                   6    
HELIX   18 AB9 GLN B  217  VAL B  242  1                                  26    
HELIX   19 AC1 VAL B  243  MET B  247  5                                   5    
HELIX   20 AC2 THR B  248  LEU B  261  1                                  14    
HELIX   21 AC3 LYS C    2  TYR C   52  1                                  51    
HELIX   22 AC4 SER C   55  ALA C   74  1                                  20    
HELIX   23 AC5 ARG C   79  THR C   92  1                                  14    
HELIX   24 AC6 THR C  103  GLY C  148  1                                  46    
HELIX   25 AC7 SER C  155  GLU C  182  1                                  28    
HELIX   26 AC8 THR C  185  THR C  198  1                                  14    
HELIX   27 AC9 GLN C  212  GLN C  217  1                                   6    
HELIX   28 AD1 GLN C  217  VAL C  242  1                                  26    
HELIX   29 AD2 VAL C  243  MET C  247  5                                   5    
HELIX   30 AD3 THR C  248  ALA C  258  1                                  11    
HELIX   31 AD4 LYS D    2  TYR D   52  1                                  51    
HELIX   32 AD5 SER D   55  ALA D   74  1                                  20    
HELIX   33 AD6 ARG D   79  THR D   92  1                                  14    
HELIX   34 AD7 THR D  103  GLY D  148  1                                  46    
HELIX   35 AD8 SER D  155  HIS D  183  1                                  29    
HELIX   36 AD9 THR D  185  THR D  198  1                                  14    
HELIX   37 AE1 GLN D  212  GLN D  217  1                                   6    
HELIX   38 AE2 GLN D  217  VAL D  243  1                                  27    
HELIX   39 AE3 LEU D  244  MET D  247  5                                   4    
HELIX   40 AE4 THR D  248  LEU D  261  1                                  14    
LINK         O   THR A  93                 K     K A 304     1555   1555  2.85  
LINK         O   THR A  93                 K     K A 303     1555   1555  2.68  
LINK         OG1 THR A  93                 K     K A 304     1555   1555  2.79  
LINK         O   ILE A  94                 K     K A 301     1555   1555  2.74  
LINK         O   ILE A  94                 K     K A 303     1555   1555  2.79  
LINK         O   GLY A  95                 K     K A 309     1555   1555  2.88  
LINK         O   GLY A  95                 K     K A 301     1555   1555  2.76  
LINK         O   TYR A  96                 K     K A 309     1555   1555  2.72  
LINK         O   THR A 199                 K     K A 304     1555   1555  2.76  
LINK         O   THR A 199                 K     K A 303     1555   1555  2.62  
LINK         OG1 THR A 199                 K     K A 304     1555   1555  2.91  
LINK         O   ILE A 200                 K     K A 301     1555   1555  2.71  
LINK         O   ILE A 200                 K     K A 303     1555   1555  2.75  
LINK         O   GLY A 201                 K     K A 309     1555   1555  2.79  
LINK         O   GLY A 201                 K     K A 301     1555   1555  2.64  
LINK         O   PHE A 202                 K     K A 309     1555   1555  2.86  
LINK         O   THR B  93                 K     K A 304     1555   1555  2.81  
LINK         O   THR B  93                 K     K A 303     1555   1555  2.68  
LINK         OG1 THR B  93                 K     K A 304     1555   1555  2.74  
LINK         O   ILE B  94                 K     K A 301     1555   1555  2.79  
LINK         O   ILE B  94                 K     K A 303     1555   1555  2.83  
LINK         O   GLY B  95                 K     K A 309     1555   1555  2.92  
LINK         O   GLY B  95                 K     K A 301     1555   1555  2.74  
LINK         O   TYR B  96                 K     K A 309     1555   1555  2.76  
LINK         O   THR B 199                 K     K A 304     1555   1555  2.85  
LINK         O   THR B 199                 K     K A 303     1555   1555  2.75  
LINK         OG1 THR B 199                 K     K A 304     1555   1555  3.04  
LINK         O   ILE B 200                 K     K A 301     1555   1555  2.82  
LINK         O   ILE B 200                 K     K A 303     1555   1555  2.86  
LINK         O   GLY B 201                 K     K A 309     1555   1555  2.78  
LINK         O   GLY B 201                 K     K A 301     1555   1555  2.75  
LINK         O   PHE B 202                 K     K A 309     1555   1555  2.83  
LINK         O   THR C  93                 K     K C 303     1555   1555  2.68  
LINK         O   THR C  93                 K     K C 304     1555   1555  2.82  
LINK         OG1 THR C  93                 K     K C 304     1555   1555  2.75  
LINK         O   ILE C  94                 K     K C 302     1555   1555  2.75  
LINK         O   ILE C  94                 K     K C 303     1555   1555  2.77  
LINK         O   GLY C  95                 K     K C 301     1555   1555  2.89  
LINK         O   GLY C  95                 K     K C 302     1555   1555  2.77  
LINK         O   TYR C  96                 K     K C 301     1555   1555  2.73  
LINK         O   THR C 199                 K     K C 303     1555   1555  2.60  
LINK         O   THR C 199                 K     K C 304     1555   1555  2.80  
LINK         OG1 THR C 199                 K     K C 304     1555   1555  2.96  
LINK         O   ILE C 200                 K     K C 302     1555   1555  2.72  
LINK         O   ILE C 200                 K     K C 303     1555   1555  2.73  
LINK         O   GLY C 201                 K     K C 301     1555   1555  2.80  
LINK         O   GLY C 201                 K     K C 302     1555   1555  2.65  
LINK         O   PHE C 202                 K     K C 301     1555   1555  2.86  
LINK         O   THR D  93                 K     K C 303     1555   1555  2.71  
LINK         O   THR D  93                 K     K C 304     1555   1555  2.90  
LINK         OG1 THR D  93                 K     K C 304     1555   1555  2.82  
LINK         O   ILE D  94                 K     K C 302     1555   1555  2.83  
LINK         O   ILE D  94                 K     K C 303     1555   1555  2.92  
LINK         O   GLY D  95                 K     K C 301     1555   1555  2.95  
LINK         O   GLY D  95                 K     K C 302     1555   1555  2.73  
LINK         O   TYR D  96                 K     K C 301     1555   1555  2.77  
LINK         O   THR D 199                 K     K C 303     1555   1555  2.79  
LINK         O   THR D 199                 K     K C 304     1555   1555  2.84  
LINK         OG1 THR D 199                 K     K C 304     1555   1555  3.00  
LINK         O   ILE D 200                 K     K C 302     1555   1555  2.84  
LINK         O   ILE D 200                 K     K C 303     1555   1555  2.89  
LINK         O   GLY D 201                 K     K C 301     1555   1555  2.83  
LINK         O   GLY D 201                 K     K C 302     1555   1555  2.78  
LINK         O   PHE D 202                 K     K C 301     1555   1555  2.84  
SITE     1 AC1 10 ILE A  94  GLY A  95  ILE A 200  GLY A 201                    
SITE     2 AC1 10   K A 303    K A 309  ILE B  94  GLY B  95                    
SITE     3 AC1 10 ILE B 200  GLY B 201                                          
SITE     1 AC2 10 THR A  93  ILE A  94  THR A 199  ILE A 200                    
SITE     2 AC2 10   K A 301    K A 304  THR B  93  ILE B  94                    
SITE     3 AC2 10 THR B 199  ILE B 200                                          
SITE     1 AC3  5 THR A  93  THR A 199    K A 303  THR B  93                    
SITE     2 AC3  5 THR B 199                                                     
SITE     1 AC4  4 ARG A   3  PHE A 246  LEU B 115  PRO B 119                    
SITE     1 AC5  6 PHE A  80  ALA A  81  PHE A  84  GLN A 215                    
SITE     2 AC5  6 PHE A 225  PHE B  16                                          
SITE     1 AC6  1 ARG A 131                                                     
SITE     1 AC7  3 LEU A  29  ALA B 176  HIS B 180                               
SITE     1 AC8  9 GLY A  95  TYR A  96  GLY A 201  PHE A 202                    
SITE     2 AC8  9   K A 301  GLY B  95  TYR B  96  GLY B 201                    
SITE     3 AC8  9 PHE B 202                                                     
SITE     1 AC9 22 THR A  92  THR A  93  ILE A 118  LEU A 122                    
SITE     2 AC9 22 PHE A 125  LEU A 197  THR A 198  THR A 199                    
SITE     3 AC9 22 LEU A 232  ILE A 235  LEU A 239  THR B  92                    
SITE     4 AC9 22 THR B  93  ILE B 118  LEU B 122  PHE B 125                    
SITE     5 AC9 22 LEU B 197  THR B 198  THR B 199  LEU B 232                    
SITE     6 AC9 22 ILE B 235  LEU B 239                                          
SITE     1 AD1  3 LEU A 115  ARG B   3  PHE B 246                               
SITE     1 AD2  6 PHE A  16  ARG B  79  PHE B  80  ALA B  81                    
SITE     2 AD2  6 PHE B  84  GLN B 215                                          
SITE     1 AD3  1 ARG B 131                                                     
SITE     1 AD4  9 GLY C  95  TYR C  96  GLY C 201  PHE C 202                    
SITE     2 AD4  9   K C 302  GLY D  95  TYR D  96  GLY D 201                    
SITE     3 AD4  9 PHE D 202                                                     
SITE     1 AD5 10 ILE C  94  GLY C  95  ILE C 200  GLY C 201                    
SITE     2 AD5 10   K C 301    K C 303  ILE D  94  GLY D  95                    
SITE     3 AD5 10 ILE D 200  GLY D 201                                          
SITE     1 AD6 10 THR C  93  ILE C  94  THR C 199  ILE C 200                    
SITE     2 AD6 10   K C 302    K C 304  THR D  93  ILE D  94                    
SITE     3 AD6 10 THR D 199  ILE D 200                                          
SITE     1 AD7  5 THR C  93  THR C 199    K C 303  THR D  93                    
SITE     2 AD7  5 THR D 199                                                     
SITE     1 AD8  4 ARG C   3  PHE C 238  PHE C 246  LEU D 115                    
SITE     1 AD9 22 THR C  92  THR C  93  ILE C 118  LEU C 122                    
SITE     2 AD9 22 PHE C 125  LEU C 197  THR C 198  THR C 199                    
SITE     3 AD9 22 LEU C 232  ILE C 235  LEU C 239  THR D  92                    
SITE     4 AD9 22 THR D  93  ILE D 118  LEU D 122  PHE D 125                    
SITE     5 AD9 22 LEU D 197  THR D 198  THR D 199  LEU D 232                    
SITE     6 AD9 22 ILE D 235  LEU D 239                                          
SITE     1 AE1  1 ARG C 131                                                     
SITE     1 AE2  4 PHE C 112  PHE C 186  VAL D  25  ALA D  28                    
SITE     1 AE3  3 LEU C 115  ARG D   3  PHE D 246                               
SITE     1 AE4  6 PHE C  16  ARG D  79  PHE D  80  ALA D  81                    
SITE     2 AE4  6 PHE D  84  GLN D 215                                          
SITE     1 AE5  3 GLU C 254  ARG D 131  LEU D 135                               
SITE     1 AE6  5 LEU C  29  GLY D 105  PHE D 112  SER D 169                    
SITE     2 AE6  5 HIS D 180                                                     
CRYST1   45.070  204.500  239.320  90.00  90.00  90.00 P 2 21 21    16          
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      0.022188  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004890  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004179        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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