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Database: PDB
Entry: 4TWK
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HEADER    TRANSPORT PROTEIN                       30-JUN-14   4TWK              
TITLE     CRYSTAL STRUCTURE OF HUMAN TWO PORE DOMAIN POTASSIUM ION CHANNEL TREK1
TITLE    2 (K2P2.1)                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM CHANNEL SUBFAMILY K MEMBER 2;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 26-300;                                       
COMPND   5 SYNONYM: OUTWARD RECTIFYING POTASSIUM CHANNEL PROTEIN TREK-1,TREK-1  
COMPND   6 K(+) CHANNEL SUBUNIT,TWO PORE DOMAIN POTASSIUM CHANNEL TREK-1,TWO    
COMPND   7 PORE POTASSIUM CHANNEL TPKC1;                                        
COMPND   8 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: KCNK2, TREK, TREK1;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFB-CT10HF-LIC                            
KEYWDS    ION CHANNEL, MEMBRANE PROTEIN, K2P, TRANSPORT PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.W.PIKE,Y.Y.DONG,A.TESSITORE,S.GOUBIN,C.STRAIN-DAMERELL,           
AUTHOR   2 S.MUKHOPADHYAY,K.KUPINSKA,D.WANG,R.CHALK,G.BERRIDGE,M.GRIEBEN,       
AUTHOR   3 L.SHRESTHA,J.H.ANG,A.MACKENZIE,A.QUIGLEY,S.R.BUSHELL,C.A.SHINTRE,    
AUTHOR   4 B.FAUST,A.CHU,L.DONG,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,         
AUTHOR   5 C.BOUNTRA,N.A.BURGESS-BROWN,E.P.CARPENTER                            
REVDAT   2   29-JUL-20 4TWK    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE                                     
REVDAT   1   06-AUG-14 4TWK    0                                                
JRNL        AUTH   A.C.W.PIKE,Y.Y.DONG,A.TESSITORE,S.GOUBIN,C.STRAIN-DAMERELL,  
JRNL        AUTH 2 S.MUKHOPADHYAY,K.KUPINSKA,D.WANG,R.CHALK,G.BERRIDGE,         
JRNL        AUTH 3 M.GRIEBEN,L.SHRESTHA,J.H.ANG,A.MACKENZIE,A.QUIGLEY,          
JRNL        AUTH 4 S.R.BUSHELL,C.A.SHINTRE,B.FAUST,A.CHU,L.DONG,F.VON DELFT,    
JRNL        AUTH 5 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,N.A.BURGESS-BROWN,      
JRNL        AUTH 6 E.P.CARPENTER                                                
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TWO PORE DOMAIN POTASSIUM ION     
JRNL        TITL 2 CHANNEL TREK1 (K2P2.1)                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 31710                          
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)  : 0.232                          
REMARK   3   R VALUE            (WORKING SET)  : 0.231                          
REMARK   3   FREE R VALUE                      : 0.258                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1607                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.40                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2700                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1897                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2549                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1901                   
REMARK   3   BIN FREE R VALUE                        : 0.1829                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.59                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 151                      
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            : 3746                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 168                                     
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.16                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 113.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.07280                                             
REMARK   3    B22 (A**2) : -20.66700                                            
REMARK   3    B33 (A**2) : 28.73970                                             
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) : 0.522               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.288               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.230               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.298               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.237               
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      : 0.891                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4005   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5468   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1769   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 53     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 571    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4005   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 592    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4902   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.22                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.71                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|38 - 408}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   14.2202   -1.5973  -24.9434           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3902 T22:   -0.2826                                    
REMARK   3     T33:   -0.3534 T12:    0.0587                                    
REMARK   3     T13:   -0.0463 T23:   -0.0544                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9839 L22:    2.3819                                    
REMARK   3     L33:    7.3875 L12:   -0.8042                                    
REMARK   3     L13:   -1.3281 L23:    0.8396                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2022 S12:    0.1107 S13:   -0.0981                     
REMARK   3     S21:    0.0585 S22:    0.1014 S23:    0.0242                     
REMARK   3     S31:    0.0098 S32:   -0.7110 S33:    0.1008                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|42 - 750} INCLUDES NAG GLYCOSYLATION ON B95         
REMARK   3    ORIGIN FOR THE GROUP (A):   24.6670    2.8693  -17.0848           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3944 T22:   -0.3104                                    
REMARK   3     T33:   -0.3706 T12:    0.0612                                    
REMARK   3     T13:   -0.1044 T23:   -0.1166                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3033 L22:    1.8665                                    
REMARK   3     L33:    6.9659 L12:   -0.7249                                    
REMARK   3     L13:   -0.9781 L23:   -0.0063                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1476 S12:   -0.4146 S13:    0.0597                     
REMARK   3     S21:    0.2563 S22:    0.2551 S23:   -0.4413                     
REMARK   3     S31:   -0.5092 S32:    0.7804 S33:   -0.1074                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DIFFRACTION DATA WERE SEVERELY            
REMARK   3  ANISOTROPIC ALL DATA TO 2.6A WAS USED IN REFINEMENT WITHOUT         
REMARK   3  TRUNCATION. NOMINAL RESOLUTION IS 2.8A BASED ON MN (I)/SD(I)>2      
REMARK   3  CRITERIA                                                            
REMARK   4                                                                      
REMARK   4 4TWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202400.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.83600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4BW5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25M MAGNESIUM FORMATE, 0.1M SODIUM     
REMARK 280  CACODYLATE PH 6.5, 17% PEG3000, 5% PEG400, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.23500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.13500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.98750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.13500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.98750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 25620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 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 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    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     VAL A    33                                                      
REMARK 465     GLU A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     ALA A   227                                                      
REMARK 465     ILE A   228                                                      
REMARK 465     ILE A   229                                                      
REMARK 465     PHE A   230                                                      
REMARK 465     LYS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     ILE A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     GLU A   265                                                      
REMARK 465     TYR A   266                                                      
REMARK 465     LEU A   267                                                      
REMARK 465     ASP A   268                                                      
REMARK 465     PHE A   269                                                      
REMARK 465     TYR A   270                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     MET B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     LEU B    29                                                      
REMARK 465     ALA B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     ARG B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     THR B    38                                                      
REMARK 465     ILE B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     VAL B    41                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     ASN B   119                                                      
REMARK 465     THR B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     GLN B   123                                                      
REMARK 465     VAL B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     ILE B   264                                                      
REMARK 465     GLU B   265                                                      
REMARK 465     TYR B   266                                                      
REMARK 465     LEU B   267                                                      
REMARK 465     ASP B   268                                                      
REMARK 465     PHE B   269                                                      
REMARK 465     TYR B   270                                                      
REMARK 465     ASN B   303                                                      
REMARK 465     LEU B   304                                                      
REMARK 465     TYR B   305                                                      
REMARK 465     PHE B   306                                                      
REMARK 465     GLN B   307                                                      
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     THR A  38    OG1  CG2                                            
REMARK 470     ILE A  39    CG1  CG2  CD1                                       
REMARK 470     LYS A  45    CG   CD   CE   NZ                                   
REMARK 470     ILE A  80    CG1  CG2  CD1                                       
REMARK 470     SER A  96    OG                                                  
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 100    CG   OD1  OD2                                       
REMARK 470     GLU A 101    CD   OE1  OE2                                       
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 197    CG1  CG2  CD1                                       
REMARK 470     ASN A 200    CG   OD1  ND2                                       
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     ARG A 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 208    CG1  CG2  CD1                                       
REMARK 470     ILE A 209    CG1  CG2  CD1                                       
REMARK 470     LEU A 225    CG   CD1  CD2                                       
REMARK 470     TYR A 257    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 263    CG   OD1  OD2                                       
REMARK 470     ILE A 264    CG1  CG2  CD1                                       
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     LYS B  45    CD   CE   NZ                                        
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 189    CG1  CG2  CD1                                       
REMARK 470     LYS B 191    CE   NZ                                             
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 197    CG1  CG2  CD1                                       
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     THR B 204    OG1  CG2                                            
REMARK 470     LYS B 205    CD   CE   NZ                                        
REMARK 470     ILE B 206    CG1  CG2  CD1                                       
REMARK 470     ILE B 208    CG1  CG2  CD1                                       
REMARK 470     LYS B 231    CG   CD   CE   NZ                                   
REMARK 470     LYS B 271    CG   CD   CE   NZ                                   
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    PHE A 145       43.39   -140.00                                   
REMARK 500    VAL A 223      -54.59   -120.03                                   
REMARK 500    ASN B 200       79.96     46.38                                   
REMARK 500    VAL B 223      -59.51   -129.85                                   
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     37X A  403                                                       
REMARK 610     37X A  404                                                       
REMARK 610     37X A  406                                                       
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                              MG A 407  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 113   O                                                      
REMARK 620 2 GLY A 260   O    89.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 401   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 142   O                                                      
REMARK 620 2 THR A 142   OG1  65.9                                              
REMARK 620 3 THR A 251   O    69.2 109.2                                        
REMARK 620 4 THR A 251   OG1 104.1  76.4  65.0                                  
REMARK 620 5 THR B 142   O   106.4 171.3  70.2 110.3                            
REMARK 620 6 THR B 142   OG1 170.2 123.8 105.2  79.8  63.9                      
REMARK 620 7 THR B 251   O    66.4 106.3 102.2 166.7  65.9 108.2                
REMARK 620 8 THR B 251   OG1 109.9  79.4 169.2 124.7 100.4  74.0  68.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 403   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 142   O                                                      
REMARK 620 2 ILE A 143   O    70.3                                              
REMARK 620 3 THR A 251   O    61.2  80.7                                        
REMARK 620 4 ILE A 252   O   124.5  72.4  73.4                                  
REMARK 620 5 THR B 142   O    91.9 143.0  62.4  94.1                            
REMARK 620 6 ILE B 143   O   145.6 133.0 136.1  89.6  79.4                      
REMARK 620 7 THR B 251   O    62.3 127.1  95.4 156.5  62.4  84.5                
REMARK 620 8 ILE B 252   O    84.3  80.2 144.7 127.3 131.5  77.3  73.5          
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 402   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 143   O                                                      
REMARK 620 2 HOH A 509   O    96.9                                              
REMARK 620 3 HOH A 510   O    68.3  85.4                                        
REMARK 620 4 PHE B 145   O   147.6  51.3  99.3                                  
REMARK 620 5 HOH B 511   O   103.5 158.6 108.2 108.9                            
REMARK 620 N                    1     2     3     4                             
DBREF  4TWK A   26   300  UNP    O95069   KCNK2_HUMAN     26    300             
DBREF  4TWK B   26   300  UNP    O95069   KCNK2_HUMAN     26    300             
SEQADV 4TWK MET A   25  UNP  O95069              INITIATING METHIONINE          
SEQADV 4TWK ALA A  301  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK GLU A  302  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK ASN A  303  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK LEU A  304  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK TYR A  305  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK PHE A  306  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK GLN A  307  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK MET B   25  UNP  O95069              INITIATING METHIONINE          
SEQADV 4TWK ALA B  301  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK GLU B  302  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK ASN B  303  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK LEU B  304  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK TYR B  305  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK PHE B  306  UNP  O95069              EXPRESSION TAG                 
SEQADV 4TWK GLN B  307  UNP  O95069              EXPRESSION TAG                 
SEQRES   1 A  283  MET PRO THR VAL LEU ALA SER ARG VAL GLU SER ASP THR          
SEQRES   2 A  283  THR ILE ASN VAL MET LYS TRP LYS THR VAL SER THR ILE          
SEQRES   3 A  283  PHE LEU VAL VAL VAL LEU TYR LEU ILE ILE GLY ALA THR          
SEQRES   4 A  283  VAL PHE LYS ALA LEU GLU GLN PRO HIS GLU ILE SER GLN          
SEQRES   5 A  283  ARG THR THR ILE VAL ILE GLN LYS GLN THR PHE ILE SER          
SEQRES   6 A  283  GLN HIS SER CYS VAL ASN SER THR GLU LEU ASP GLU LEU          
SEQRES   7 A  283  ILE GLN GLN ILE VAL ALA ALA ILE ASN ALA GLY ILE ILE          
SEQRES   8 A  283  PRO LEU GLY ASN THR SER ASN GLN ILE SER HIS TRP ASP          
SEQRES   9 A  283  LEU GLY SER SER PHE PHE PHE ALA GLY THR VAL ILE THR          
SEQRES  10 A  283  THR ILE GLY PHE GLY ASN ILE SER PRO ARG THR GLU GLY          
SEQRES  11 A  283  GLY LYS ILE PHE CYS ILE ILE TYR ALA LEU LEU GLY ILE          
SEQRES  12 A  283  PRO LEU PHE GLY PHE LEU LEU ALA GLY VAL GLY ASP GLN          
SEQRES  13 A  283  LEU GLY THR ILE PHE GLY LYS GLY ILE ALA LYS VAL GLU          
SEQRES  14 A  283  ASP THR PHE ILE LYS TRP ASN VAL SER GLN THR LYS ILE          
SEQRES  15 A  283  ARG ILE ILE SER THR ILE ILE PHE ILE LEU PHE GLY CYS          
SEQRES  16 A  283  VAL LEU PHE VAL ALA LEU PRO ALA ILE ILE PHE LYS HIS          
SEQRES  17 A  283  ILE GLU GLY TRP SER ALA LEU ASP ALA ILE TYR PHE VAL          
SEQRES  18 A  283  VAL ILE THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL          
SEQRES  19 A  283  ALA GLY GLY SER ASP ILE GLU TYR LEU ASP PHE TYR LYS          
SEQRES  20 A  283  PRO VAL VAL TRP PHE TRP ILE LEU VAL GLY LEU ALA TYR          
SEQRES  21 A  283  PHE ALA ALA VAL LEU SER MET ILE GLY ASP TRP LEU ARG          
SEQRES  22 A  283  VAL ILE SER ALA GLU ASN LEU TYR PHE GLN                      
SEQRES   1 B  283  MET PRO THR VAL LEU ALA SER ARG VAL GLU SER ASP THR          
SEQRES   2 B  283  THR ILE ASN VAL MET LYS TRP LYS THR VAL SER THR ILE          
SEQRES   3 B  283  PHE LEU VAL VAL VAL LEU TYR LEU ILE ILE GLY ALA THR          
SEQRES   4 B  283  VAL PHE LYS ALA LEU GLU GLN PRO HIS GLU ILE SER GLN          
SEQRES   5 B  283  ARG THR THR ILE VAL ILE GLN LYS GLN THR PHE ILE SER          
SEQRES   6 B  283  GLN HIS SER CYS VAL ASN SER THR GLU LEU ASP GLU LEU          
SEQRES   7 B  283  ILE GLN GLN ILE VAL ALA ALA ILE ASN ALA GLY ILE ILE          
SEQRES   8 B  283  PRO LEU GLY ASN THR SER ASN GLN ILE SER HIS TRP ASP          
SEQRES   9 B  283  LEU GLY SER SER PHE PHE PHE ALA GLY THR VAL ILE THR          
SEQRES  10 B  283  THR ILE GLY PHE GLY ASN ILE SER PRO ARG THR GLU GLY          
SEQRES  11 B  283  GLY LYS ILE PHE CYS ILE ILE TYR ALA LEU LEU GLY ILE          
SEQRES  12 B  283  PRO LEU PHE GLY PHE LEU LEU ALA GLY VAL GLY ASP GLN          
SEQRES  13 B  283  LEU GLY THR ILE PHE GLY LYS GLY ILE ALA LYS VAL GLU          
SEQRES  14 B  283  ASP THR PHE ILE LYS TRP ASN VAL SER GLN THR LYS ILE          
SEQRES  15 B  283  ARG ILE ILE SER THR ILE ILE PHE ILE LEU PHE GLY CYS          
SEQRES  16 B  283  VAL LEU PHE VAL ALA LEU PRO ALA ILE ILE PHE LYS HIS          
SEQRES  17 B  283  ILE GLU GLY TRP SER ALA LEU ASP ALA ILE TYR PHE VAL          
SEQRES  18 B  283  VAL ILE THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL          
SEQRES  19 B  283  ALA GLY GLY SER ASP ILE GLU TYR LEU ASP PHE TYR LYS          
SEQRES  20 B  283  PRO VAL VAL TRP PHE TRP ILE LEU VAL GLY LEU ALA TYR          
SEQRES  21 B  283  PHE ALA ALA VAL LEU SER MET ILE GLY ASP TRP LEU ARG          
SEQRES  22 B  283  VAL ILE SER ALA GLU ASN LEU TYR PHE GLN                      
HET      K  A 401       1                                                       
HET      K  A 402       1                                                       
HET    37X  A 403      18                                                       
HET    37X  A 404      25                                                       
HET    37X  A 405      39                                                       
HET    37X  A 406      29                                                       
HET     MG  A 407       1                                                       
HET      K  B 403       1                                                       
HET    NAG  B 401      14                                                       
HET    37X  B 402      39                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     37X OCTYL GLUCOSE NEOPENTYL GLYCOL                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3    K    3(K 1+)                                                      
FORMUL   5  37X    5(C27 H52 O12)                                               
FORMUL   9   MG    MG 2+                                                        
FORMUL  11  NAG    C8 H15 N O6                                                  
FORMUL  13  HOH   *27(H2 O)                                                     
HELIX    1 AA1 THR A   38  HIS A   91  1                                  54    
HELIX    2 AA2 ASN A   95  GLY A  113  1                                  19    
HELIX    3 AA3 ASP A  128  THR A  141  1                                  14    
HELIX    4 AA4 THR A  152  TRP A  199  1                                  48    
HELIX    5 AA5 SER A  202  VAL A  223  1                                  22    
HELIX    6 AA6 SER A  237  THR A  250  1                                  14    
HELIX    7 AA7 PRO A  272  PHE A  306  1                                  35    
HELIX    8 AA8 LYS B   43  HIS B   91  1                                  49    
HELIX    9 AA9 ASN B   95  ALA B  112  1                                  18    
HELIX   10 AB1 ASP B  128  THR B  141  1                                  14    
HELIX   11 AB2 THR B  152  TRP B  199  1                                  48    
HELIX   12 AB3 SER B  202  VAL B  223  1                                  22    
HELIX   13 AB4 VAL B  223  ILE B  233  1                                  11    
HELIX   14 AB5 SER B  237  THR B  250  1                                  14    
HELIX   15 AB6 PRO B  272  GLU B  302  1                                  31    
SSBOND   1 CYS A   93    CYS B   93                          1555   1555  2.04  
LINK         ND2 ASN B  95                 C1  NAG B 401     1555   1555  1.44  
LINK         O   GLY A 113                MG    MG A 407     1555   1555  2.36  
LINK         O   THR A 142                 K     K A 401     1555   1555  2.74  
LINK         OG1 THR A 142                 K     K A 401     1555   1555  2.70  
LINK         O   THR A 142                 K     K B 403     1555   1555  3.07  
LINK         O   ILE A 143                 K     K A 402     1555   1555  3.43  
LINK         O   ILE A 143                 K     K B 403     1555   1555  3.00  
LINK         O   THR A 251                 K     K A 401     1555   1555  2.73  
LINK         OG1 THR A 251                 K     K A 401     1555   1555  2.89  
LINK         O   THR A 251                 K     K B 403     1555   1555  3.04  
LINK         O   ILE A 252                 K     K B 403     1555   1555  2.96  
LINK         O   GLY A 260                MG    MG A 407     1555   1555  2.19  
LINK         K     K A 401                 O   THR B 142     1555   1555  2.64  
LINK         K     K A 401                 OG1 THR B 142     1555   1555  3.00  
LINK         K     K A 401                 O   THR B 251     1555   1555  2.80  
LINK         K     K A 401                 OG1 THR B 251     1555   1555  2.73  
LINK         K     K A 402                 O   HOH A 509     1555   1555  2.81  
LINK         K     K A 402                 O   HOH A 510     1555   1555  3.26  
LINK         K     K A 402                 O   PHE B 145     1555   1555  3.37  
LINK         K     K A 402                 O   HOH B 511     1555   1555  3.24  
LINK         O   THR B 142                 K     K B 403     1555   1555  2.93  
LINK         O   ILE B 143                 K     K B 403     1555   1555  2.60  
LINK         O   THR B 251                 K     K B 403     1555   1555  2.78  
LINK         O   ILE B 252                 K     K B 403     1555   1555  2.87  
CISPEP   1 LEU A  117    GLY A  118          0       -10.43                     
CRYST1   74.470  105.975  128.270  90.00  90.00  90.00 P 21 21 21    8          
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      0.013428  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007796        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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