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Database: PDB
Entry: 6RV2
LinkDB: 6RV2
Original site: 6RV2 
HEADER    MEMBRANE PROTEIN                        30-MAY-19   6RV2              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN TWO PORE DOMAIN POTASSIUM ION CHANNEL  
TITLE    2 TASK-1 (K2P3.1) IN A CLOSED CONFORMATION                             
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                                                      
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_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 6RV2    1       JRNL                                     
REVDAT   1   07-AUG-19 6RV2    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.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36373                          
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)  : 0.254                          
REMARK   3   R VALUE            (WORKING SET)  : 0.253                          
REMARK   3   FREE R VALUE                      : 0.257                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.830                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1756                           
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) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.05                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 35.86                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 728                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2303                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 689                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2288                   
REMARK   3   BIN FREE R VALUE                        : 0.2558                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.36                     
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            : 8009                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 426                                     
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.54                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -13.82380                                            
REMARK   3    B22 (A**2) : 10.72830                                             
REMARK   3    B33 (A**2) : 3.09550                                              
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) : 0.510               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.417               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.392               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 1.499               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.400               
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      : 0.808                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.841                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8623   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11696  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3090   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 1405   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8623   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1155   ; 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   : 10204  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.90                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.03                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.91                    
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):    2.8402  -40.8535   25.7508           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3993 T22:    0.0125                                    
REMARK   3     T33:   -0.1857 T12:    0.0051                                    
REMARK   3     T13:    0.0138 T23:    0.1461                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6606 L22:    1.6699                                    
REMARK   3     L33:    2.1926 L12:   -0.4943                                    
REMARK   3     L13:    0.3103 L23:   -0.3695                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0601 S12:    0.0939 S13:   -0.2428                     
REMARK   3     S21:   -0.1763 S22:   -0.1832 S23:   -0.1138                     
REMARK   3     S31:    0.0786 S32:    0.1330 S33:    0.1231                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|1 - 261}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.4415  -37.2744   29.3343           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3471 T22:    0.0129                                    
REMARK   3     T33:   -0.0825 T12:   -0.0089                                    
REMARK   3     T13:   -0.0039 T23:    0.1504                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4165 L22:    1.1463                                    
REMARK   3     L33:    1.3738 L12:    0.0583                                    
REMARK   3     L13:    0.1829 L23:   -0.4329                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0148 S12:   -0.0132 S13:    0.0371                     
REMARK   3     S21:   -0.0417 S22:   -0.0520 S23:    0.2460                     
REMARK   3     S31:    0.0482 S32:   -0.2038 S33:    0.0372                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|1 - 304}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.2901   22.8180   33.0410           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4537 T22:    0.0394                                    
REMARK   3     T33:   -0.1763 T12:    0.0273                                    
REMARK   3     T13:    0.0294 T23:    0.0184                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.9376 L22:    2.2300                                    
REMARK   3     L33:    2.1015 L12:    0.1376                                    
REMARK   3     L13:    0.2300 L23:   -0.7173                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0490 S12:    0.0534 S13:    0.2297                     
REMARK   3     S21:   -0.1019 S22:   -0.0482 S23:    0.0750                     
REMARK   3     S31:   -0.0606 S32:   -0.1080 S33:    0.0972                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {D|1 - 261}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.6297   19.1023   36.7996           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4173 T22:   -0.0131                                    
REMARK   3     T33:   -0.1060 T12:    0.0084                                    
REMARK   3     T13:    0.0362 T23:    0.0947                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.0878 L22:    1.6474                                    
REMARK   3     L33:    2.2730 L12:    0.1747                                    
REMARK   3     L13:   -0.0610 L23:   -0.5885                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0013 S12:   -0.1963 S13:   -0.0272                     
REMARK   3     S21:    0.0071 S22:    0.1433 S23:   -0.0460                     
REMARK   3     S31:    0.0372 S32:    0.0922 S33:   -0.1420                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINED AGAINST STARANISO                 
REMARK   3  ANISOTROPICALLY TRUNCATED DATA                                      
REMARK   4                                                                      
REMARK   4 6RV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102563.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-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 MAR 15, 2019,       
REMARK 200                                   STARANISO 2.2.19                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36417                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.668                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.21500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 37.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.02100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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   (%): 73.14                                     
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, 32% V/V   
REMARK 280  PEG400, 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      102.39500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      119.17000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.39500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      119.17000            
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: 13530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 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: 12950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24460 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     ALA A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     ASN A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     TYR A   262                                                      
REMARK 465     PHE A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     MET B   149                                                      
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     ALA C   258                                                      
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     GLU A  37    OE1  OE2                                            
REMARK 470     GLN A  56    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  64    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  70    CD   CE   NZ                                        
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 147    CG   CD1  CD2                                       
REMARK 470     ASP A 153    CG   OD1  OD2                                       
REMARK 470     PHE A 164    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     LYS A 255    CE   NZ                                             
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  56    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  62    CG   CD1  CD2                                       
REMARK 470     LEU B 147    CG   CD1  CD2                                       
REMARK 470     GLN B 219    CG   CD   OE1  NE2                                  
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     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 260    CG   OD1  ND2                                       
REMARK 470     LEU B 261    CG   CD1  CD2                                       
REMARK 470     ARG C   3    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C  32    CD   OE1  OE2                                       
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     ARG C  79    NE   CZ   NH1  NH2                                  
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 210    CG   CD   CE   NZ                                   
REMARK 470     LYS C 255    CE   NZ                                             
REMARK 470     ARG C 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  32    OE1  OE2                                            
REMARK 470     LEU D  48    CG   CD1  CD2                                       
REMARK 470     ARG D  51    NE   CZ   NH1  NH2                                  
REMARK 470     ASN D  53    CG   OD1  ND2                                       
REMARK 470     GLN D  56    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  70    CG   CD   CE   NZ                                   
REMARK 470     LYS D  73    CG   CD   CE   NZ                                   
REMARK 470     ARG D  79    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 145    CG   CD   CE   NZ                                   
REMARK 470     LEU D 147    CG   CD1  CD2                                       
REMARK 470     MET D 149    CG   SD   CE                                        
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     PHE D 164    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     HIS D 183    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 210    NZ                                                  
REMARK 470     LYS D 255    CG   CD   CE   NZ                                   
REMARK 470     ARG D 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 259    CG   CD   OE1  OE2                                  
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     -158.68    -81.65                                   
REMARK 500    ARG B  79     -155.98    -82.15                                   
REMARK 500    THR B 199       19.64     59.81                                   
REMARK 500    LEU B 208       34.22     71.51                                   
REMARK 500    GLN B 217       77.71   -117.60                                   
REMARK 500    ARG C  79     -155.36    -82.55                                   
REMARK 500    GLN C 217       78.14   -116.66                                   
REMARK 500    ARG D  79     -159.15    -82.89                                   
REMARK 500    GLN D 217       78.45   -118.04                                   
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  303                                                       
REMARK 610     PC1 B  304                                                       
REMARK 610     DMU C  306                                                       
REMARK 610     PC1 D  601                                                       
REMARK 610     PC1 D  604                                                       
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 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  93   O                                                      
REMARK 620 2 ILE A  94   O    74.0                                              
REMARK 620 3 THR A 199   O    67.7  88.6                                        
REMARK 620 4 ILE A 200   O   130.3  73.9  74.6                                  
REMARK 620 5 THR B  93   O   107.1 154.2  69.0  87.4                            
REMARK 620 6 ILE B  94   O   153.9 116.2 133.2  75.5  74.6                      
REMARK 620 7 THR B 199   O    68.5 131.8 103.5 154.3  68.5  88.9                
REMARK 620 8 ILE B 200   O    87.1  74.7 153.0 119.2 130.8  73.8  74.2          
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 304   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  93   O                                                      
REMARK 620 2 THR A  93   OG1  65.4                                              
REMARK 620 3 THR A 199   O    64.5 110.1                                        
REMARK 620 4 THR A 199   OG1 105.7  83.3  67.3                                  
REMARK 620 5 THR B  93   O    95.0 158.5  65.5 111.9                            
REMARK 620 6 THR B  93   OG1 161.5 132.3 106.8  84.1  66.6                      
REMARK 620 7 THR B 199   O    62.5  99.1  97.9 164.6  62.2 104.8                
REMARK 620 8 THR B 199   OG1 103.5  77.8 158.4 134.3  99.6  79.0  60.7          
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 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A  94   O                                                      
REMARK 620 2 GLY A  95   O    70.4                                              
REMARK 620 3 ILE A 200   O    76.2 136.9                                        
REMARK 620 4 GLY A 201   O    80.6  77.2  71.0                                  
REMARK 620 5 ILE B  94   O   124.4 145.1  77.1 132.8                            
REMARK 620 6 GLY B  95   O   146.7 117.3  78.7  70.7  69.5                      
REMARK 620 7 ILE B 200   O    77.2  78.3 120.1 151.3  75.6 135.1                
REMARK 620 8 GLY B 201   O   133.4  70.6 149.8 114.1  79.2  75.6  70.8          
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    77.5                                              
REMARK 620 3 GLY A 201   O    74.0  93.4                                        
REMARK 620 4 PHE A 202   O   133.5  71.5  74.2                                  
REMARK 620 5 GLY B  95   O   110.4 155.6  68.2  87.7                            
REMARK 620 6 TYR B  96   O   155.7 106.6 128.6  68.6  76.0                      
REMARK 620 7 GLY B 201   O    68.3 129.7 110.5 156.3  73.5  92.4                
REMARK 620 8 PHE B 202   O    88.9  69.3 158.2 110.6 132.1  71.0  74.1          
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    75.2                                              
REMARK 620 3 THR C 199   O    68.0  89.3                                        
REMARK 620 4 ILE C 200   O   131.8  74.7  74.9                                  
REMARK 620 5 THR D  93   O   105.4 154.0  67.8  87.0                            
REMARK 620 6 ILE D  94   O   152.8 117.4 132.1  75.3  74.1                      
REMARK 620 7 THR D 199   O    67.5 133.0 101.8 152.3  66.9  88.3                
REMARK 620 8 ILE D 200   O    87.0  75.7 153.6 120.2 130.1  74.2  74.7          
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  65.5                                              
REMARK 620 3 THR C 199   O    64.0 108.7                                        
REMARK 620 4 THR C 199   OG1 104.7  82.1  66.4                                  
REMARK 620 5 THR D  93   O    95.8 160.3  65.1 110.2                            
REMARK 620 6 THR D  93   OG1 162.4 132.0 105.4  81.8  66.6                      
REMARK 620 7 THR D 199   O    62.9 100.4  97.8 163.8  63.5 107.2                
REMARK 620 8 THR D 199   OG1 105.8  78.4 161.2 132.3 102.2  80.0  63.5          
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 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE C  94   O                                                      
REMARK 620 2 GLY C  95   O    70.2                                              
REMARK 620 3 ILE C 200   O    76.1 136.9                                        
REMARK 620 4 GLY C 201   O    80.4  77.2  71.2                                  
REMARK 620 5 ILE D  94   O   122.7 145.6  76.2 133.4                            
REMARK 620 6 GLY D  95   O   146.4 119.0  77.7  71.5  69.6                      
REMARK 620 7 ILE D 200   O    76.5  79.0 118.5 151.3  74.5 135.3                
REMARK 620 8 GLY D 201   O   133.4  71.6 149.4 115.8  79.2  77.0  70.8          
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    78.1                                              
REMARK 620 3 GLY C 201   O    74.4  93.9                                        
REMARK 620 4 PHE C 202   O   134.2  71.5  74.4                                  
REMARK 620 5 GLY D  95   O   109.7 156.2  68.0  88.3                            
REMARK 620 6 TYR D  96   O   154.9 106.8 128.5  68.9  76.0                      
REMARK 620 7 GLY D 201   O    68.5 130.2 110.4 155.5  72.4  91.4                
REMARK 620 8 PHE D 202   O    88.9  69.9 159.1 110.9 131.1  70.6  73.6          
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 302                   
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 Y01 A 301                 
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 DMU B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 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 DMU C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 D 604                 
DBREF  6RV2 A    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV2 B    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV2 C    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
DBREF  6RV2 D    1   259  UNP    O14649   KCNK3_HUMAN      1    259             
SEQADV 6RV2 ASN A  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 LEU A  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 TYR A  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 PHE A  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 GLN A  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 ASN B  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 LEU B  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 TYR B  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 PHE B  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 GLN B  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 ASN C  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 LEU C  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 TYR C  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 PHE C  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 GLN C  264  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 ASN D  260  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 LEU D  261  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 TYR D  262  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 PHE D  263  UNP  O14649              EXPRESSION TAG                 
SEQADV 6RV2 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 302       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      22                                                       
HET    PC1  A 308      32                                                       
HET      K  A 309       1                                                       
HET    Y01  A 301      35                                                       
HET    Y01  B 302      35                                                       
HET    DMU  B 303      20                                                       
HET    PC1  B 304      18                                                       
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    DMU  C 306      22                                                       
HET    PC1  D 601      38                                                       
HET    Y01  D 602      35                                                       
HET    Y01  D 603      35                                                       
HET    PC1  D 604      21                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     Y01 CHOLESTEROL HEMISUCCINATE                                        
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE                                     
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETSYN     DMU DECYLMALTOSIDE                                                   
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   5    K    8(K 1+)                                                      
FORMUL   8  Y01    7(C31 H50 O4)                                                
FORMUL  10  DMU    3(C22 H42 O11)                                               
FORMUL  11  PC1    4(C44 H88 N O8 P)                                            
FORMUL  27  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  209  ASP A  211  5                                   3    
HELIX    8 AA8 GLN A  212  GLN A  217  1                                   6    
HELIX    9 AA9 GLN A  217  VAL A  243  1                                  27    
HELIX   10 AB1 VAL A  243  ASP A  257  1                                  15    
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  209  ASP B  211  5                                   3    
HELIX   18 AB9 GLN B  212  GLN B  217  1                                   6    
HELIX   19 AC1 GLN B  217  VAL B  243  1                                  27    
HELIX   20 AC2 LEU B  244  MET B  247  5                                   4    
HELIX   21 AC3 THR B  248  LEU B  261  1                                  14    
HELIX   22 AC4 LYS C    2  TYR C   52  1                                  51    
HELIX   23 AC5 SER C   55  ALA C   74  1                                  20    
HELIX   24 AC6 ARG C   79  THR C   92  1                                  14    
HELIX   25 AC7 THR C  103  GLY C  148  1                                  46    
HELIX   26 AC8 SER C  155  GLU C  182  1                                  28    
HELIX   27 AC9 THR C  185  THR C  198  1                                  14    
HELIX   28 AD1 GLN C  212  GLN C  217  1                                   6    
HELIX   29 AD2 GLN C  217  VAL C  243  1                                  27    
HELIX   30 AD3 VAL C  243  ASP C  257  1                                  15    
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  GLU D  182  1                                  28    
HELIX   36 AD9 THR D  185  THR D  198  1                                  14    
HELIX   37 AE1 GLN D  209  ASP D  211  5                                   3    
HELIX   38 AE2 GLN D  212  GLN D  217  1                                   6    
HELIX   39 AE3 GLN D  217  VAL D  243  1                                  27    
HELIX   40 AE4 VAL D  243  LEU D  261  1                                  19    
LINK         O   THR A  93                 K     K A 303     1555   1555  2.68  
LINK         O   THR A  93                 K     K A 304     1555   1555  2.90  
LINK         OG1 THR A  93                 K     K A 304     1555   1555  2.81  
LINK         O   ILE A  94                 K     K A 302     1555   1555  2.70  
LINK         O   ILE A  94                 K     K A 303     1555   1555  2.84  
LINK         O   GLY A  95                 K     K A 309     1555   1555  2.86  
LINK         O   GLY A  95                 K     K A 302     1555   1555  2.74  
LINK         O   TYR A  96                 K     K A 309     1555   1555  2.77  
LINK         O   THR A 199                 K     K A 303     1555   1555  2.71  
LINK         O   THR A 199                 K     K A 304     1555   1555  2.70  
LINK         OG1 THR A 199                 K     K A 304     1555   1555  2.71  
LINK         O   ILE A 200                 K     K A 302     1555   1555  2.74  
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 302     1555   1555  2.71  
LINK         O   PHE A 202                 K     K A 309     1555   1555  2.85  
LINK         O   THR B  93                 K     K A 303     1555   1555  2.64  
LINK         O   THR B  93                 K     K A 304     1555   1555  2.89  
LINK         OG1 THR B  93                 K     K A 304     1555   1555  2.74  
LINK         O   ILE B  94                 K     K A 302     1555   1555  2.73  
LINK         O   ILE B  94                 K     K A 303     1555   1555  2.83  
LINK         O   GLY B  95                 K     K A 309     1555   1555  2.89  
LINK         O   GLY B  95                 K     K A 302     1555   1555  2.79  
LINK         O   TYR B  96                 K     K A 309     1555   1555  2.84  
LINK         O   THR B 199                 K     K A 303     1555   1555  2.71  
LINK         O   THR B 199                 K     K A 304     1555   1555  2.94  
LINK         OG1 THR B 199                 K     K A 304     1555   1555  2.98  
LINK         O   ILE B 200                 K     K A 302     1555   1555  2.74  
LINK         O   ILE B 200                 K     K A 303     1555   1555  2.76  
LINK         O   GLY B 201                 K     K A 309     1555   1555  2.79  
LINK         O   GLY B 201                 K     K A 302     1555   1555  2.76  
LINK         O   PHE B 202                 K     K A 309     1555   1555  2.85  
LINK         O   THR C  93                 K     K C 303     1555   1555  2.66  
LINK         O   THR C  93                 K     K C 304     1555   1555  2.91  
LINK         OG1 THR C  93                 K     K C 304     1555   1555  2.79  
LINK         O   ILE C  94                 K     K C 302     1555   1555  2.72  
LINK         O   ILE C  94                 K     K C 303     1555   1555  2.81  
LINK         O   GLY C  95                 K     K C 301     1555   1555  2.84  
LINK         O   GLY C  95                 K     K C 302     1555   1555  2.73  
LINK         O   TYR C  96                 K     K C 301     1555   1555  2.78  
LINK         O   THR C 199                 K     K C 303     1555   1555  2.71  
LINK         O   THR C 199                 K     K C 304     1555   1555  2.76  
LINK         OG1 THR C 199                 K     K C 304     1555   1555  2.77  
LINK         O   ILE C 200                 K     K C 302     1555   1555  2.76  
LINK         O   ILE C 200                 K     K C 303     1555   1555  2.75  
LINK         O   GLY C 201                 K     K C 301     1555   1555  2.78  
LINK         O   GLY C 201                 K     K C 302     1555   1555  2.72  
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  2.86  
LINK         OG1 THR D  93                 K     K C 304     1555   1555  2.75  
LINK         O   ILE D  94                 K     K C 302     1555   1555  2.77  
LINK         O   ILE D  94                 K     K C 303     1555   1555  2.83  
LINK         O   GLY D  95                 K     K C 301     1555   1555  2.92  
LINK         O   GLY D  95                 K     K C 302     1555   1555  2.74  
LINK         O   TYR D  96                 K     K C 301     1555   1555  2.83  
LINK         O   THR D 199                 K     K C 303     1555   1555  2.74  
LINK         O   THR D 199                 K     K C 304     1555   1555  2.85  
LINK         OG1 THR D 199                 K     K C 304     1555   1555  2.91  
LINK         O   ILE D 200                 K     K C 302     1555   1555  2.77  
LINK         O   ILE D 200                 K     K C 303     1555   1555  2.73  
LINK         O   GLY D 201                 K     K C 301     1555   1555  2.83  
LINK         O   GLY D 201                 K     K C 302     1555   1555  2.72  
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 302    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  5 ARG A   3  PHE A 238  PHE A 246  LEU B 115                    
SITE     2 AC4  5 PRO B 119                                                     
SITE     1 AC5  6 ARG A  79  PHE A  80  ALA A  81  GLN A 215                    
SITE     2 AC5  6 PHE A 225  PHE B  16                                          
SITE     1 AC6  2 ARG A 131  ILE A 132                                          
SITE     1 AC7  4 GLY A 105  PHE A 112  ALA A 176  ALA B  28                    
SITE     1 AC8  9 GLY A  95  TYR A  96  GLY A 201  PHE A 202                    
SITE     2 AC8  9   K A 302  GLY B  95  TYR B  96  GLY B 201                    
SITE     3 AC8  9 PHE B 202                                                     
SITE     1 AC9  3 ARG B   3  PHE B 238  PHE B 246                               
SITE     1 AD1  6 PHE A  16  ARG B  79  PHE B  80  ALA B  81                    
SITE     2 AD1  6 GLN B 215  PHE B 225                                          
SITE     1 AD2  2 LYS A   2  ARG B 131                                          
SITE     1 AD3  4 GLY B 105  PHE B 112  SER B 169  HIS B 180                    
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  3 PHE C 246  LEU D 115  PRO D 119                               
SITE     1 AD9  1 ARG C 131                                                     
SITE     1 AE1  5 GLY C 105  PHE C 112  SER C 169  ALA D  28                    
SITE     2 AE1  5 LEU D  29                                                     
SITE     1 AE2  4 LEU C 115  ARG D   3  PHE D 238  PHE D 246                    
SITE     1 AE3  5 PHE C  16  ARG D  79  PHE D  80  ALA D  81                    
SITE     2 AE3  5 GLN D 215                                                     
SITE     1 AE4  4 GLY D 105  PHE D 112  SER D 169  HIS D 180                    
CRYST1   45.140  204.790  238.340  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      0.022153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004883  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004196        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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