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Database: PDB
Entry: 3SYQ
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Original site: 3SYQ 
HEADER    METAL TRANSPORT                         18-JUL-11   3SYQ              
TITLE     CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+ CHANNEL  
TITLE    2 GIRK2 (KIR3.2) R201A MUTANT IN COMPLEX WITH PIP2                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 2;  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 52-380;                                       
COMPND   5 SYNONYM: GIRK-2, INWARD RECTIFIER K(+) CHANNEL KIR3.2, POTASSIUM     
COMPND   6 CHANNEL, INWARDLY RECTIFYING SUBFAMILY J MEMBER 6;                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: GIRK2, KCNJ6, KCNJ7, W;                                        
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SMD1163;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZ                                     
KEYWDS    ION CHANNEL, POTASSIUM CHANNEL, INWARD RECTIFICATION, SODIUM BINDING, 
KEYWDS   2 PIP2 BINDING, G PROTEIN BINDING, METAL TRANSPORT                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.WHORTON,R.MACKINNON                                               
REVDAT   1   12-OCT-11 3SYQ    0                                                
JRNL        AUTH   M.R.WHORTON,R.MACKINNON                                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE MAMMALIAN GIRK2 K(+) CHANNEL AND    
JRNL        TITL 2 GATING REGULATION BY G PROTEINS, PIP(2), AND SODIUM.         
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 147   199 2011              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   21962516                                                     
JRNL        DOI    10.1016/J.CELL.2011.07.046                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11814                          
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) : 0.301                           
REMARK   3   R VALUE            (WORKING SET) : 0.299                           
REMARK   3   FREE R VALUE                     : 0.323                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 575                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.44                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 76                           
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 7.43                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 4                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4490                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 138.37                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.18000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.770         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.780         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 112.639       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.842                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.858                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4619 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6290 ; 1.019 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   578 ; 5.281 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   179 ;36.317 ;23.575       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   728 ;17.508 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.003 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   746 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3385 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2901 ; 0.257 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4658 ; 0.477 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1718 ; 0.452 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1632 ; 0.820 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    100       A     179      1                      
REMARK   3           1     B    100       B     179      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    477 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):    477 ; 0.010 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    203       A     225      4                      
REMARK   3           1     B    203       B     225      4                      
REMARK   3           2     A    238       A     244      4                      
REMARK   3           2     B    238       B     244      4                      
REMARK   3           3     A    260       A     308      4                      
REMARK   3           3     B    260       B     308      4                      
REMARK   3           4     A    325       A     382      6                      
REMARK   3           4     B    325       B     382      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    621 ; 0.360 ; 0.500           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    378 ; 0.330 ; 5.000           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    621 ; 1.460 ; 2.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):    378 ; 0.910 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    55        A   377                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4154  33.0676 -16.7333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6048 T22:   0.8337                                     
REMARK   3      T33:   0.6430 T12:   0.1066                                     
REMARK   3      T13:   0.3828 T23:  -0.3558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4271 L22:   7.8977                                     
REMARK   3      L33:   2.7487 L12:   1.4746                                     
REMARK   3      L13:   0.3614 L23:  -1.0183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4083 S12:  -0.5336 S13:   0.1969                       
REMARK   3      S21:   1.1245 S22:  -0.1470 S23:   0.9345                       
REMARK   3      S31:  -0.3751 S32:  -0.4722 S33:   0.5554                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    55        B   378                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9362  33.6209 -39.6322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4934 T22:   0.7049                                     
REMARK   3      T33:   0.5787 T12:   0.1844                                     
REMARK   3      T13:  -0.0566 T23:  -0.1279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1890 L22:  10.8280                                     
REMARK   3      L33:   2.6777 L12:   0.0653                                     
REMARK   3      L13:   0.1125 L23:   3.0247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0655 S12:   0.1226 S13:   0.2935                       
REMARK   3      S21:  -1.0134 S22:  -0.5368 S23:   0.9212                       
REMARK   3      S31:  -0.4641 S32:  -0.4946 S33:   0.4713                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : WITH TLS ADDED                                      
REMARK   4                                                                      
REMARK   4 3SYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066818.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.034                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14690                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.432                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2E4F                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES SODIUM, PH 7.25, 0.5 M       
REMARK 280  SODIUM CHLORIDE, 25% PEG400, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.68800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.68800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.80250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      104.24550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.80250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      104.24550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.68800            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.80250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      104.24550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.68800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.80250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      104.24550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -58.68800            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 K      K A 501  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 503  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 504  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 502  LIES ON A SPECIAL POSITION.                          
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    50                                                      
REMARK 465     ALA A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     ARG A    53                                                      
REMARK 465     LYS A    54                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     ASN A    71                                                      
REMARK 465     VAL A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     THR A    75                                                      
REMARK 465     TYR A    76                                                      
REMARK 465     ARG A    77                                                      
REMARK 465     TYR A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     THR A    80                                                      
REMARK 465     TYR A   118                                                      
REMARK 465     ILE A   119                                                      
REMARK 465     ARG A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     MET A   123                                                      
REMARK 465     ASP A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     ILE A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     ASP A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     SER A   130                                                      
REMARK 465     TRP A   131                                                      
REMARK 465     THR A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     GLY A   347                                                      
REMARK 465     ARG A   378                                                      
REMARK 465     ALA A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     SER A   383                                                      
REMARK 465     LEU A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     LEU A   387                                                      
REMARK 465     PHE A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     MET B    50                                                      
REMARK 465     ALA B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     ARG B    53                                                      
REMARK 465     LYS B    54                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     HIS B    68                                                      
REMARK 465     HIS B    69                                                      
REMARK 465     GLY B    70                                                      
REMARK 465     ASN B    71                                                      
REMARK 465     VAL B    72                                                      
REMARK 465     ARG B    73                                                      
REMARK 465     GLU B    74                                                      
REMARK 465     THR B    75                                                      
REMARK 465     TYR B    76                                                      
REMARK 465     ARG B    77                                                      
REMARK 465     TYR B    78                                                      
REMARK 465     LEU B    79                                                      
REMARK 465     THR B    80                                                      
REMARK 465     ASP B    81                                                      
REMARK 465     TYR B   118                                                      
REMARK 465     ILE B   119                                                      
REMARK 465     ARG B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     ASP B   122                                                      
REMARK 465     MET B   123                                                      
REMARK 465     ASP B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     ILE B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     ASP B   128                                                      
REMARK 465     PRO B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     TRP B   131                                                      
REMARK 465     THR B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     ALA B   379                                                      
REMARK 465     GLU B   380                                                      
REMARK 465     SER B   381                                                      
REMARK 465     ASN B   382                                                      
REMARK 465     SER B   383                                                      
REMARK 465     LEU B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     VAL B   386                                                      
REMARK 465     LEU B   387                                                      
REMARK 465     PHE B   388                                                      
REMARK 465     GLN B   389                                                      
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     ARG A  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  88    CG   OD1  OD2                                       
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     MET A 111    CG   SD   CE                                        
REMARK 470     LEU A 115    CG   CD1  CD2                                       
REMARK 470     ILE A 116    CG1  CG2  CD1                                       
REMARK 470     VAL A 135    CG1  CG2                                            
REMARK 470     ASN A 137    CG   OD1  ND2                                       
REMARK 470     LEU A 138    CG   CD1  CD2                                       
REMARK 470     ASN A 139    CG   OD1  ND2                                       
REMARK 470     VAL A 161    CG1  CG2                                            
REMARK 470     ILE A 162    CG1  CG2  CD1                                       
REMARK 470     THR A 163    OG1  CG2                                            
REMARK 470     LYS A 165    CG   CD   CE   NZ                                   
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 170    CG1  CG2  CD1                                       
REMARK 470     PHE A 186    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 199    CG   CD   CE   NZ                                   
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     ARG A 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 231    CG   OD1  ND2                                       
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 348    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 349    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 350    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  55    CG1  CG2  CD1                                       
REMARK 470     ASP B  88    CG   OD1  OD2                                       
REMARK 470     LYS B  90    CG   CD   CE   NZ                                   
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 111    CG   SD   CE                                        
REMARK 470     LEU B 115    CG   CD1  CD2                                       
REMARK 470     ILE B 116    CG1  CG2  CD1                                       
REMARK 470     VAL B 135    CG1  CG2                                            
REMARK 470     ASN B 137    CG   OD1  ND2                                       
REMARK 470     LEU B 138    CG   CD1  CD2                                       
REMARK 470     ASN B 139    CG   OD1  ND2                                       
REMARK 470     VAL B 161    CG1  CG2                                            
REMARK 470     ILE B 162    CG1  CG2  CD1                                       
REMARK 470     THR B 163    OG1  CG2                                            
REMARK 470     LYS B 165    CG   CD   CE   NZ                                   
REMARK 470     GLU B 168    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 170    CG1  CG2  CD1                                       
REMARK 470     PHE B 186    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 200    CG   CD   CE   NZ                                   
REMARK 470     HIS B 233    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     GLU B 303    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 345    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 350    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 374    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 377    CG   OD1  ND2                                       
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    ASN A  66       49.90    -88.40                                   
REMARK 500    LEU A  95      -37.49    -39.82                                   
REMARK 500    ILE A 234       75.16     46.29                                   
REMARK 500    LEU A 257       57.34   -114.35                                   
REMARK 500    LYS A 301       35.42    -79.44                                   
REMARK 500    GLU A 303       67.11   -103.02                                   
REMARK 500    SER A 363      107.86    -58.61                                   
REMARK 500    MET B 191      -78.81    -57.43                                   
REMARK 500    SER B 232       98.71    -68.14                                   
REMARK 500    ASP B 270        3.62    -67.51                                   
REMARK 500    VAL B 276      -74.93   -113.13                                   
REMARK 500    ASP B 346       80.33     52.65                                   
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     PIO A  400                                                       
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 504   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 154   OG1                                                    
REMARK 620 2 THR B 154   O   111.3                                              
REMARK 620 3 THR A 154   O    59.9  75.5                                        
REMARK 620 4 THR B 154   OG1  84.2  55.3 101.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 502   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 155   O                                                      
REMARK 620 2 GLY B 156   O    92.6                                              
REMARK 620 3 GLY A 156   O    62.0  81.5                                        
REMARK 620 4 ILE B 155   O    73.3  61.0 119.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 503   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 155   O                                                      
REMARK 620 2 THR A 154   O   124.6                                              
REMARK 620 3 ILE A 155   O    76.0  72.8                                        
REMARK 620 4 THR B 154   O    69.7  71.7  99.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 156   O                                                      
REMARK 620 2 GLY B 156   O    75.5                                              
REMARK 620 3 TYR B 157   O   133.6  74.3                                        
REMARK 620 4 TYR A 157   O    73.3  91.1  72.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIO A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 502                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 503                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 504                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SYA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER            
REMARK 900 K+ CHANNEL GIRK2 (KIR3.2) IN COMPLEX WITH SODIUM AND PIP2            
REMARK 900 RELATED ID: 3SYC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER            
REMARK 900 K+ CHANNEL GIRK2 (KIR3.2) D228N MUTANT                               
REMARK 900 RELATED ID: 3SYO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER            
REMARK 900 K+ CHANNEL GIRK2 (KIR3.2) IN COMPLEX WITH SODIUM                     
REMARK 900 RELATED ID: 3SYP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER            
REMARK 900 K+ CHANNEL GIRK2 (KIR3.2) R201A MUTANT                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP P48542 S260T, I313M, AND M344L ARE NATURAL VARIANTS.             
DBREF  3SYQ A   52   380  UNP    P48542   IRK6_MOUSE      52    380             
DBREF  3SYQ B   52   380  UNP    P48542   IRK6_MOUSE      52    380             
SEQADV 3SYQ MET A   50  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ALA A   51  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ALA A  201  UNP  P48542    ARG   201 ENGINEERED MUTATION            
SEQADV 3SYQ THR A  260  UNP  P48542    SER   260 SEE REMARK 999                 
SEQADV 3SYQ MET A  313  UNP  P48542    ILE   313 SEE REMARK 999                 
SEQADV 3SYQ LEU A  344  UNP  P48542    MET   344 SEE REMARK 999                 
SEQADV 3SYQ SER A  381  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ASN A  382  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ SER A  383  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ LEU A  384  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ GLU A  385  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ VAL A  386  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ LEU A  387  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ PHE A  388  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ GLN A  389  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ MET B   50  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ALA B   51  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ALA B  201  UNP  P48542    ARG   201 ENGINEERED MUTATION            
SEQADV 3SYQ THR B  260  UNP  P48542    SER   260 SEE REMARK 999                 
SEQADV 3SYQ MET B  313  UNP  P48542    ILE   313 SEE REMARK 999                 
SEQADV 3SYQ LEU B  344  UNP  P48542    MET   344 SEE REMARK 999                 
SEQADV 3SYQ SER B  381  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ ASN B  382  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ SER B  383  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ LEU B  384  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ GLU B  385  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ VAL B  386  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ LEU B  387  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ PHE B  388  UNP  P48542              EXPRESSION TAG                 
SEQADV 3SYQ GLN B  389  UNP  P48542              EXPRESSION TAG                 
SEQRES   1 A  340  MET ALA LYS ARG LYS ILE GLN ARG TYR VAL ARG LYS ASP          
SEQRES   2 A  340  GLY LYS CYS ASN VAL HIS HIS GLY ASN VAL ARG GLU THR          
SEQRES   3 A  340  TYR ARG TYR LEU THR ASP ILE PHE THR THR LEU VAL ASP          
SEQRES   4 A  340  LEU LYS TRP ARG PHE ASN LEU LEU ILE PHE VAL MET VAL          
SEQRES   5 A  340  TYR THR VAL THR TRP LEU PHE PHE GLY MET ILE TRP TRP          
SEQRES   6 A  340  LEU ILE ALA TYR ILE ARG GLY ASP MET ASP HIS ILE GLU          
SEQRES   7 A  340  ASP PRO SER TRP THR PRO CYS VAL THR ASN LEU ASN GLY          
SEQRES   8 A  340  PHE VAL SER ALA PHE LEU PHE SER ILE GLU THR GLU THR          
SEQRES   9 A  340  THR ILE GLY TYR GLY TYR ARG VAL ILE THR ASP LYS CYS          
SEQRES  10 A  340  PRO GLU GLY ILE ILE LEU LEU LEU ILE GLN SER VAL LEU          
SEQRES  11 A  340  GLY SER ILE VAL ASN ALA PHE MET VAL GLY CYS MET PHE          
SEQRES  12 A  340  VAL LYS ILE SER GLN PRO LYS LYS ALA ALA GLU THR LEU          
SEQRES  13 A  340  VAL PHE SER THR HIS ALA VAL ILE SER MET ARG ASP GLY          
SEQRES  14 A  340  LYS LEU CYS LEU MET PHE ARG VAL GLY ASP LEU ARG ASN          
SEQRES  15 A  340  SER HIS ILE VAL GLU ALA SER ILE ARG ALA LYS LEU ILE          
SEQRES  16 A  340  LYS SER LYS GLN THR SER GLU GLY GLU PHE ILE PRO LEU          
SEQRES  17 A  340  ASN GLN THR ASP ILE ASN VAL GLY TYR TYR THR GLY ASP          
SEQRES  18 A  340  ASP ARG LEU PHE LEU VAL SER PRO LEU ILE ILE SER HIS          
SEQRES  19 A  340  GLU ILE ASN GLN GLN SER PRO PHE TRP GLU ILE SER LYS          
SEQRES  20 A  340  ALA GLN LEU PRO LYS GLU GLU LEU GLU ILE VAL VAL ILE          
SEQRES  21 A  340  LEU GLU GLY MET VAL GLU ALA THR GLY MET THR CYS GLN          
SEQRES  22 A  340  ALA ARG SER SER TYR ILE THR SER GLU ILE LEU TRP GLY          
SEQRES  23 A  340  TYR ARG PHE THR PRO VAL LEU THR LEU GLU ASP GLY PHE          
SEQRES  24 A  340  TYR GLU VAL ASP TYR ASN SER PHE HIS GLU THR TYR GLU          
SEQRES  25 A  340  THR SER THR PRO SER LEU SER ALA LYS GLU LEU ALA GLU          
SEQRES  26 A  340  LEU ALA ASN ARG ALA GLU SER ASN SER LEU GLU VAL LEU          
SEQRES  27 A  340  PHE GLN                                                      
SEQRES   1 B  340  MET ALA LYS ARG LYS ILE GLN ARG TYR VAL ARG LYS ASP          
SEQRES   2 B  340  GLY LYS CYS ASN VAL HIS HIS GLY ASN VAL ARG GLU THR          
SEQRES   3 B  340  TYR ARG TYR LEU THR ASP ILE PHE THR THR LEU VAL ASP          
SEQRES   4 B  340  LEU LYS TRP ARG PHE ASN LEU LEU ILE PHE VAL MET VAL          
SEQRES   5 B  340  TYR THR VAL THR TRP LEU PHE PHE GLY MET ILE TRP TRP          
SEQRES   6 B  340  LEU ILE ALA TYR ILE ARG GLY ASP MET ASP HIS ILE GLU          
SEQRES   7 B  340  ASP PRO SER TRP THR PRO CYS VAL THR ASN LEU ASN GLY          
SEQRES   8 B  340  PHE VAL SER ALA PHE LEU PHE SER ILE GLU THR GLU THR          
SEQRES   9 B  340  THR ILE GLY TYR GLY TYR ARG VAL ILE THR ASP LYS CYS          
SEQRES  10 B  340  PRO GLU GLY ILE ILE LEU LEU LEU ILE GLN SER VAL LEU          
SEQRES  11 B  340  GLY SER ILE VAL ASN ALA PHE MET VAL GLY CYS MET PHE          
SEQRES  12 B  340  VAL LYS ILE SER GLN PRO LYS LYS ALA ALA GLU THR LEU          
SEQRES  13 B  340  VAL PHE SER THR HIS ALA VAL ILE SER MET ARG ASP GLY          
SEQRES  14 B  340  LYS LEU CYS LEU MET PHE ARG VAL GLY ASP LEU ARG ASN          
SEQRES  15 B  340  SER HIS ILE VAL GLU ALA SER ILE ARG ALA LYS LEU ILE          
SEQRES  16 B  340  LYS SER LYS GLN THR SER GLU GLY GLU PHE ILE PRO LEU          
SEQRES  17 B  340  ASN GLN THR ASP ILE ASN VAL GLY TYR TYR THR GLY ASP          
SEQRES  18 B  340  ASP ARG LEU PHE LEU VAL SER PRO LEU ILE ILE SER HIS          
SEQRES  19 B  340  GLU ILE ASN GLN GLN SER PRO PHE TRP GLU ILE SER LYS          
SEQRES  20 B  340  ALA GLN LEU PRO LYS GLU GLU LEU GLU ILE VAL VAL ILE          
SEQRES  21 B  340  LEU GLU GLY MET VAL GLU ALA THR GLY MET THR CYS GLN          
SEQRES  22 B  340  ALA ARG SER SER TYR ILE THR SER GLU ILE LEU TRP GLY          
SEQRES  23 B  340  TYR ARG PHE THR PRO VAL LEU THR LEU GLU ASP GLY PHE          
SEQRES  24 B  340  TYR GLU VAL ASP TYR ASN SER PHE HIS GLU THR TYR GLU          
SEQRES  25 B  340  THR SER THR PRO SER LEU SER ALA LYS GLU LEU ALA GLU          
SEQRES  26 B  340  LEU ALA ASN ARG ALA GLU SER ASN SER LEU GLU VAL LEU          
SEQRES  27 B  340  PHE GLN                                                      
HET    PIO  A 400      31                                                       
HET      K  A 501       1                                                       
HET      K  A 502       1                                                       
HET      K  A 503       1                                                       
HET      K  A 504       1                                                       
HETNAM     PIO L-ALPHA-D-MYOPHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE,              
HETNAM   2 PIO  D(+)SN1,2DI-O-OCTANOYLGLYCERYL                                  
HETNAM       K POTASSIUM ION                                                    
HETSYN     PIO L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-DIPHOSPHATE,             
HETSYN   2 PIO  DIOCTANOYL; L-ALPHA-PHOSPHATIDYLINOSITOL 4,5-                   
HETSYN   3 PIO  DIPHOSPHATE SODIUM SALT; PIP2; 1,2-DIACYL-SN-GLYCERO-           
HETSYN   4 PIO  3-PHOSPHO-(1-D-MYO-INOSITOL4,5-BISPHOSPHATE);                   
HETSYN   5 PIO  TRIPHOSPHOINOSITIDE                                             
FORMUL   3  PIO    C25 H49 O19 P3                                               
FORMUL   4    K    4(K 1+)                                                      
HELIX    1   1 ILE A   82  ASP A   88  1                                   7    
HELIX    2   2 LYS A   90  ILE A  116  1                                  27    
HELIX    3   3 GLY A  140  THR A  153  1                                  14    
HELIX    4   4 CYS A  166  GLN A  197  1                                  32    
HELIX    5   5 SER A  368  ASN A  377  1                                  10    
HELIX    6   6 ILE B   82  LEU B   89  1                                   8    
HELIX    7   7 LYS B   90  ILE B  116  1                                  27    
HELIX    8   8 GLY B  140  THR B  153  1                                  14    
HELIX    9   9 CYS B  166  SER B  196  1                                  31    
HELIX   10  10 SER B  368  ARG B  378  1                                  11    
SHEET    1   A 3 LEU A 205  PHE A 207  0                                        
SHEET    2   A 3 LYS A 219  ASP A 228 -1  O  GLY A 227   N  VAL A 206           
SHEET    3   A 3 LEU A 279  GLU A 284 -1  O  HIS A 283   N  LEU A 222           
SHEET    1   B 4 LEU A 205  PHE A 207  0                                        
SHEET    2   B 4 LYS A 219  ASP A 228 -1  O  GLY A 227   N  VAL A 206           
SHEET    3   B 4 ALA A 211  ARG A 216 -1  N  ARG A 216   O  LYS A 219           
SHEET    4   B 4 ILE A 332  TRP A 334  1  O  LEU A 333   N  ALA A 211           
SHEET    1   C 3 PHE A 254  ILE A 262  0                                        
SHEET    2   C 3 GLU A 236  GLN A 248 -1  N  LYS A 247   O  ILE A 255           
SHEET    3   C 3 ARG A 272  PHE A 274 -1  O  LEU A 273   N  ALA A 237           
SHEET    1   D 4 PHE A 254  ILE A 262  0                                        
SHEET    2   D 4 GLU A 236  GLN A 248 -1  N  LYS A 247   O  ILE A 255           
SHEET    3   D 4 LEU A 304  MET A 313 -1  O  GLU A 305   N  ILE A 244           
SHEET    4   D 4 THR A 320  ILE A 328 -1  O  TYR A 327   N  ILE A 306           
SHEET    1   E 2 TYR A 336  PHE A 338  0                                        
SHEET    2   E 2 THR A 359  GLU A 361 -1  O  TYR A 360   N  ARG A 337           
SHEET    1   F 2 LEU A 342  THR A 343  0                                        
SHEET    2   F 2 GLU A 350  VAL A 351 -1  O  GLU A 350   N  THR A 343           
SHEET    1   G 3 LEU B 205  PHE B 207  0                                        
SHEET    2   G 3 LYS B 219  ASP B 228 -1  O  GLY B 227   N  VAL B 206           
SHEET    3   G 3 LEU B 279  GLU B 284 -1  O  HIS B 283   N  LEU B 222           
SHEET    1   H 4 LEU B 205  PHE B 207  0                                        
SHEET    2   H 4 LYS B 219  ASP B 228 -1  O  GLY B 227   N  VAL B 206           
SHEET    3   H 4 ALA B 211  ARG B 216 -1  N  SER B 214   O  CYS B 221           
SHEET    4   H 4 ILE B 332  TRP B 334  1  O  LEU B 333   N  ALA B 211           
SHEET    1   I 4 ILE B 234  VAL B 235  0                                        
SHEET    2   I 4 LEU B 304  VAL B 314 -1  O  MET B 313   N  VAL B 235           
SHEET    3   I 4 ILE B 239  LYS B 245 -1  N  ILE B 244   O  GLU B 305           
SHEET    4   I 4 GLN B 259  ILE B 262 -1  O  ILE B 262   N  ALA B 241           
SHEET    1   J 3 ILE B 234  VAL B 235  0                                        
SHEET    2   J 3 LEU B 304  VAL B 314 -1  O  MET B 313   N  VAL B 235           
SHEET    3   J 3 THR B 320  ILE B 328 -1  O  SER B 325   N  VAL B 308           
SHEET    1   K 2 LYS B 247  GLN B 248  0                                        
SHEET    2   K 2 PHE B 254  ILE B 255 -1  O  ILE B 255   N  LYS B 247           
SHEET    1   L 2 TYR B 336  PHE B 338  0                                        
SHEET    2   L 2 THR B 359  GLU B 361 -1  O  TYR B 360   N  ARG B 337           
SHEET    1   M 2 LEU B 342  LEU B 344  0                                        
SHEET    2   M 2 TYR B 349  VAL B 351 -1  O  GLU B 350   N  THR B 343           
SSBOND   1 CYS A  134    CYS A  166                          1555   1555  2.03  
SSBOND   2 CYS B  134    CYS B  166                          1555   1555  2.03  
LINK         OG1 THR A 154                 K     K A 504     1555   1555  2.72  
LINK         O   ILE A 155                 K     K A 502     1555   1555  2.75  
LINK         O   ILE B 155                 K     K A 503     1555   1555  2.77  
LINK         O   GLY B 156                 K     K A 502     1555   1555  2.81  
LINK         O   THR A 154                 K     K A 503     1555   1555  2.82  
LINK         O   ILE A 155                 K     K A 503     1555   1555  2.82  
LINK         O   THR B 154                 K     K A 504     1555   1555  2.82  
LINK         O   THR A 154                 K     K A 504     1555   1555  2.87  
LINK         O   GLY A 156                 K     K A 502     1555   1555  2.92  
LINK         O   GLY A 156                 K     K A 501     1555   1555  2.99  
LINK         O   ILE B 155                 K     K A 502     1555   1555  3.00  
LINK         OG1 THR B 154                 K     K A 504     1555   1555  3.01  
LINK         O   GLY B 156                 K     K A 501     1555   1555  3.11  
LINK         O   THR B 154                 K     K A 503     1555   1555  3.12  
LINK         O   TYR B 157                 K     K A 501     1555   1555  3.25  
LINK         O   TYR A 157                 K     K A 501     1555   1555  3.46  
SITE     1 AC1  4 LYS A  90  TRP A  91  ARG A  92  LYS A 194                    
SITE     1 AC2  5 GLY A 156  TYR A 157    K A 502  GLY B 156                    
SITE     2 AC2  5 TYR B 157                                                     
SITE     1 AC3  6 ILE A 155  GLY A 156    K A 501    K A 503                    
SITE     2 AC3  6 ILE B 155  GLY B 156                                          
SITE     1 AC4  6 THR A 154  ILE A 155    K A 502    K A 504                    
SITE     2 AC4  6 THR B 154  ILE B 155                                          
SITE     1 AC5  3 THR A 154    K A 503  THR B 154                               
CRYST1   87.605  208.491  117.376  90.00  90.00  90.00 C 2 2 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      0.011415  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004796  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008520        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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