GenomeNet

Database: PDB
Entry: 1ORQ
LinkDB: 1ORQ
Original site: 1ORQ 
HEADER    MEMBRANE PROTEIN                        14-MAR-03   1ORQ              
TITLE     X-RAY STRUCTURE OF A VOLTAGE-DEPENDENT POTASSIUM CHANNEL IN COMPLEX   
TITLE    2 WITH AN FAB                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6E1 FAB LIGHT CHAIN;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 6E1 FAB HEAVY CHAIN;                                       
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: POTASSIUM CHANNEL;                                         
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: KVAP;                                                      
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 OTHER_DETAILS: MOUSE HYBRIDOMA;                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   8 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   9 ORGANISM_TAXID: 10090;                                               
SOURCE  10 OTHER_DETAILS: MOUSE HYBRIDOMA;                                      
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE  13 ORGANISM_TAXID: 56636;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    POTASSIUM CHANNEL, VOLTAGE-DEPENDENT, KVAP, FAB COMPLEX, MEMBRANE     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.JIANG,A.LEE,J.CHEN,V.RUTA,M.CADENE,B.T.CHAIT,R.MACKINNON            
REVDAT   3   13-JUL-11 1ORQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1ORQ    1       VERSN                                    
REVDAT   1   06-MAY-03 1ORQ    0                                                
JRNL        AUTH   Y.JIANG,A.LEE,J.CHEN,V.RUTA,M.CADENE,B.T.CHAIT,R.MACKINNON   
JRNL        TITL   X-RAY STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL            
JRNL        REF    NATURE                        V. 423    33 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12721618                                                     
JRNL        DOI    10.1038/NATURE01580                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22476                          
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 SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1150                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3329                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 176                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5040                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.81000                                             
REMARK   3    B22 (A**2) : -2.81000                                             
REMARK   3    B33 (A**2) : 5.63000                                              
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.49                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.89                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.25                                                 
REMARK   3   BSOL        : 26.80                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ORQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018601.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.937                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB CODE 1BAF                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, CADMIUM CHLORIDE, SODIUM         
REMARK 280  ACETATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       94.71950            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       75.23950            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       94.71950            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       75.23950            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       94.71950            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       75.23950            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       94.71950            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       75.23950            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       94.71950            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       75.23950            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       94.71950            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       75.23950            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       94.71950            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       75.23950            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       94.71950            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       94.71950            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       75.23950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE CHANNEL FUNCTIONS AS TETRAMER. THE REMAINDER OF THE      
REMARK 300 BIOLOGICAL ASSEMBLY IS GENERATED BY THE FOUR FOLD AXIS: -X -Y Z, -Y  
REMARK 300 X Z, Y -X Z.                                                         
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 41530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 117430 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -456.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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      378.87800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000     -189.43900            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      189.43900            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 86560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 231790 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -962.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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      378.87800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000     -189.43900            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      189.43900            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      378.87800            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000     -189.43900            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000      189.43900            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000      189.43900            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
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 C   1  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K C   2  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K C   3  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K C   4  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K C   5  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K C   6  LIES ON A SPECIAL POSITION.                          
REMARK 375 CD    CD A 216  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   152    CD     CD B   220    15545     1.99            
REMARK 500   NH1  ARG A    62     OE2  GLU A    82     5755     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   2       79.20    -62.10                                   
REMARK 500    SER A  12       68.28   -118.48                                   
REMARK 500    VAL A  19      147.21   -176.78                                   
REMARK 500    PRO A  45      151.61    -49.54                                   
REMARK 500    THR A  52      -59.33     51.03                                   
REMARK 500    ALA A  56     -171.92    -67.76                                   
REMARK 500    SER A  57     -120.18    -44.06                                   
REMARK 500    SER A  68      171.36    171.30                                   
REMARK 500    SER A  71      119.51   -160.20                                   
REMARK 500    SER A  78      129.59   -171.52                                   
REMARK 500    GLU A  82       -7.78    -42.54                                   
REMARK 500    ALA A  85     -162.04    177.94                                   
REMARK 500    SER A  93      -90.40   -127.29                                   
REMARK 500    ASP A 111      120.44    -34.81                                   
REMARK 500    ASN A 139       78.09     21.37                                   
REMARK 500    ASP A 144      109.44    -55.05                                   
REMARK 500    GLU A 188       23.72    -77.89                                   
REMARK 500    PRO B  14      131.09    -37.56                                   
REMARK 500    SER B  15       76.83     54.97                                   
REMARK 500    LEU B  32      172.33    178.30                                   
REMARK 500    TYR B  33      163.09     67.89                                   
REMARK 500    LYS B  65      -38.46    -29.03                                   
REMARK 500    ASN B  77       65.30     60.67                                   
REMARK 500    SER B  85       77.35     40.42                                   
REMARK 500    THR B  88      -34.01    -39.22                                   
REMARK 500    VAL B 100     -146.14   -111.27                                   
REMARK 500    PRO B 131      164.45    -37.13                                   
REMARK 500    VAL B 132      179.55    -57.06                                   
REMARK 500    ASP B 135       66.16   -106.77                                   
REMARK 500    SER B 161       -2.93     61.17                                   
REMARK 500    SER B 163       12.84    -65.81                                   
REMARK 500    GLN B 176     -101.82    -90.54                                   
REMARK 500    SER B 177      -84.29    -89.18                                   
REMARK 500    SER B 190      -37.78    -34.86                                   
REMARK 500    ARG B 218     -157.23   -132.46                                   
REMARK 500    MET C  22      128.58     53.87                                   
REMARK 500    LEU C  26       26.71    -75.97                                   
REMARK 500    GLU C  28        2.32    -69.90                                   
REMARK 500    GLU C  53      106.68    -50.96                                   
REMARK 500    LEU C  55      -47.03    170.42                                   
REMARK 500    ASP C  62       -8.08    -55.49                                   
REMARK 500    ASP C  72      -65.91    -94.61                                   
REMARK 500    LYS C  79        7.22    -67.69                                   
REMARK 500    LEU C 121      -81.62    -53.07                                   
REMARK 500    SER C 132      -80.98    -38.88                                   
REMARK 500    ARG C 133       65.70    -59.27                                   
REMARK 500    SER C 135      -24.63    175.25                                   
REMARK 500    ASP C 146       -3.49    -57.68                                   
REMARK 500    GLU C 172      -32.71   -138.04                                   
REMARK 500    SER C 179      -35.73     69.52                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CD A 216  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A  62   NH1                                                    
REMARK 620 2 ARG A  62   NH2  56.9                                              
REMARK 620 3 GLU A  82   OE1 117.2 110.4                                        
REMARK 620 4 GLU A  82   OE2 118.1 151.1  43.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 220  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 178   OD2                                                    
REMARK 620 2 ASP B 178   OD1  66.0                                              
REMARK 620 3 ASP A 152   OD2 132.0 122.0                                        
REMARK 620 4 HIS A 190   ND1  99.7 116.7 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C   1   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 199   O                                                      
REMARK 620 2   K C   2   K    95.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C   2   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 198   O                                                      
REMARK 620 2   K C   3   K   106.6                                              
REMARK 620 3 VAL C 197   O    64.1  55.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C   3   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL C 197   O                                                      
REMARK 620 2   K C   4   K   115.3                                              
REMARK 620 3 THR C 196   O    75.8  47.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C   4   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 196   OG1                                                    
REMARK 620 2 THR C 196   O    64.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C   7  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 185   OD1                                                    
REMARK 620 2 ASP C 185   OD2  51.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C   9  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 133   NH1                                                    
REMARK 620 2 ARG C 133   NH2  50.4                                              
REMARK 620 3 ARG C 133   NE   48.1  47.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 2                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 9                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 216                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 217                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 220                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 218                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ORS   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF THE KVAP POTASSIUM CHANNEL VOLTAGE                
REMARK 900 SENSOR IN COMPLEX WITH AN FAB                                        
DBREF  1ORQ A  110   215  UNP    P01837   KAC_MOUSE        1    106             
DBREF  1ORQ B  120   218  UNP    P01865   GCAM_MOUSE       1     99             
DBREF  1ORQ C   18   240  UNP    Q9YDF8   KVAP_AERPE      31    253             
SEQADV 1ORQ CYS C   46  UNP  Q9YDF8    TYR    59 ENGINEERED                     
SEQRES   1 A  215  GLU ASN VAL LEU THR GLN SER PRO ALA ILE MET SER PRO          
SEQRES   2 A  215  SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA ARG          
SEQRES   3 A  215  SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN          
SEQRES   4 A  215  LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR SER THR          
SEQRES   5 A  215  SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 A  215  SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER          
SEQRES   7 A  215  VAL GLU ALA GLU ASP THR ALA THR TYR TYR CYS GLN GLN          
SEQRES   8 A  215  TYR SER GLY ASN PRO TRP THR PHE GLY GLY GLY THR LYS          
SEQRES   9 A  215  LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER          
SEQRES  10 A  215  ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY          
SEQRES  11 A  215  ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS          
SEQRES  12 A  215  ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG          
SEQRES  13 A  215  GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER          
SEQRES  14 A  215  LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU          
SEQRES  15 A  215  THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS          
SEQRES  16 A  215  GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS          
SEQRES  17 A  215  SER PHE ASN ARG ASN GLU CYS                                  
SEQRES   1 B  219  ASP VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS          
SEQRES   2 B  219  PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY          
SEQRES   3 B  219  TYR SER ILE THR SER LEU TYR ALA TRP ASN TRP ILE ARG          
SEQRES   4 B  219  GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE          
SEQRES   5 B  219  ASN TYR SER GLY TYR THR SER TYR ASN PRO SER LEU LYS          
SEQRES   6 B  219  SER ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN          
SEQRES   7 B  219  PHE PHE LEU GLN LEU HIS SER VAL THR THR GLU ASP THR          
SEQRES   8 B  219  ALA THR TYR SER CYS THR ARG GLY VAL ASP TYR PHE ALA          
SEQRES   9 B  219  MET ASP TYR TRP GLY GLN GLY ALA SER VAL THR VAL SER          
SEQRES  10 B  219  SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 B  219  PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU          
SEQRES  12 B  219  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 B  219  LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS          
SEQRES  14 B  219  THR PHE PRO ALA LEU LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 B  219  SER SER SER VAL THR VAL THR SER ASN THR TRP PRO SER          
SEQRES  16 B  219  GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 B  219  THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP                  
SEQRES   1 C  223  ILE GLY ASP VAL MET GLU HIS PRO LEU VAL GLU LEU GLY          
SEQRES   2 C  223  VAL SER TYR ALA ALA LEU LEU SER VAL ILE VAL VAL VAL          
SEQRES   3 C  223  VAL GLU CYS THR MET GLN LEU SER GLY GLU TYR LEU VAL          
SEQRES   4 C  223  ARG LEU TYR LEU VAL ASP LEU ILE LEU VAL ILE ILE LEU          
SEQRES   5 C  223  TRP ALA ASP TYR ALA TYR ARG ALA TYR LYS SER GLY ASP          
SEQRES   6 C  223  PRO ALA GLY TYR VAL LYS LYS THR LEU TYR GLU ILE PRO          
SEQRES   7 C  223  ALA LEU VAL PRO ALA GLY LEU LEU ALA LEU ILE GLU GLY          
SEQRES   8 C  223  HIS LEU ALA GLY LEU GLY LEU PHE ARG LEU VAL ARG LEU          
SEQRES   9 C  223  LEU ARG PHE LEU ARG ILE LEU LEU ILE ILE SER ARG GLY          
SEQRES  10 C  223  SER LYS PHE LEU SER ALA ILE ALA ASP ALA ALA ASP LYS          
SEQRES  11 C  223  ILE ARG PHE TYR HIS LEU PHE GLY ALA VAL MET LEU THR          
SEQRES  12 C  223  VAL LEU TYR GLY ALA PHE ALA ILE TYR ILE VAL GLU TYR          
SEQRES  13 C  223  PRO ASP PRO ASN SER SER ILE LYS SER VAL PHE ASP ALA          
SEQRES  14 C  223  LEU TRP TRP ALA VAL VAL THR ALA THR THR VAL GLY TYR          
SEQRES  15 C  223  GLY ASP VAL VAL PRO ALA THR PRO ILE GLY LYS VAL ILE          
SEQRES  16 C  223  GLY ILE ALA VAL MET LEU THR GLY ILE SER ALA LEU THR          
SEQRES  17 C  223  LEU LEU ILE GLY THR VAL SER ASN MET PHE GLN LYS ILE          
SEQRES  18 C  223  LEU VAL                                                      
HET      K  C   1       1                                                       
HET      K  C   2       1                                                       
HET      K  C   3       1                                                       
HET      K  C   4       1                                                       
HET      K  C   5       1                                                       
HET      K  C   6       1                                                       
HET     CD  C   7       1                                                       
HET     CD  C   8       1                                                       
HET     CD  C   9       1                                                       
HET     CD  A 216       1                                                       
HET     CD  A 217       1                                                       
HET     CD  B 220       1                                                       
HET     CD  A 218       1                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      CD CADMIUM ION                                                      
FORMUL   4    K    6(K 1+)                                                      
FORMUL  10   CD    7(CD 2+)                                                     
FORMUL  17  HOH   *6(H2 O)                                                      
HELIX    1   1 SER A   30  LEU A   34  5                                   5    
HELIX    2   2 GLU A   80  THR A   84  5                                   5    
HELIX    3   3 SER A  122  GLY A  129  1                                   8    
HELIX    4   4 THR A  183  GLU A  188  1                                   6    
HELIX    5   5 THR B   87  THR B   91  5                                   5    
HELIX    6   6 ASP B  101  PHE B  103  5                                   3    
HELIX    7   7 SER B  161  SER B  163  5                                   3    
HELIX    8   8 PRO B  205  SER B  208  5                                   4    
HELIX    9   9 HIS C   24  LEU C   29  1                                   6    
HELIX   10  10 LEU C   29  SER C   51  1                                  23    
HELIX   11  11 VAL C   56  LYS C   79  1                                  24    
HELIX   12  12 ASP C   82  ILE C   94  1                                  13    
HELIX   13  13 ALA C   96  GLY C  112  1                                  17    
HELIX   14  14 LEU C  115  ARG C  133  1                                  19    
HELIX   15  15 LYS C  136  VAL C  171  1                                  36    
HELIX   16  16 SER C  182  THR C  195  1                                  14    
HELIX   17  17 THR C  206  LEU C  239  1                                  34    
SHEET    1   A 2 LEU A   4  SER A   7  0                                        
SHEET    2   A 2 THR A  22  ALA A  25 -1  O  ARG A  24   N  THR A   5           
SHEET    1   B 3 VAL A  19  THR A  20  0                                        
SHEET    2   B 3 SER A  71  ILE A  76 -1  O  ILE A  76   N  VAL A  19           
SHEET    3   B 3 PHE A  63  SER A  68 -1  N  SER A  66   O  SER A  73           
SHEET    1   C 5 ASN A  54  LEU A  55  0                                        
SHEET    2   C 5 LEU A  47  TYR A  50 -1  N  TYR A  50   O  ASN A  54           
SHEET    3   C 5 HIS A  35  GLN A  39 -1  N  TRP A  36   O  TRP A  48           
SHEET    4   C 5 ALA A  85  GLN A  91 -1  O  TYR A  88   N  TYR A  37           
SHEET    5   C 5 THR A  98  PHE A  99 -1  O  THR A  98   N  GLN A  91           
SHEET    1   D 5 ASN A  54  LEU A  55  0                                        
SHEET    2   D 5 LEU A  47  TYR A  50 -1  N  TYR A  50   O  ASN A  54           
SHEET    3   D 5 HIS A  35  GLN A  39 -1  N  TRP A  36   O  TRP A  48           
SHEET    4   D 5 ALA A  85  GLN A  91 -1  O  TYR A  88   N  TYR A  37           
SHEET    5   D 5 LYS A 104  LEU A 105 -1  O  LEU A 105   N  ALA A  85           
SHEET    1   E 4 THR A 115  PHE A 119  0                                        
SHEET    2   E 4 ALA A 131  PHE A 140 -1  O  VAL A 134   N  PHE A 119           
SHEET    3   E 4 TYR A 174  LEU A 182 -1  O  TYR A 174   N  PHE A 140           
SHEET    4   E 4 VAL A 160  TRP A 164 -1  N  SER A 163   O  SER A 177           
SHEET    1   F 4 SER A 154  ARG A 156  0                                        
SHEET    2   F 4 ASN A 146  ILE A 151 -1  N  ILE A 151   O  SER A 154           
SHEET    3   F 4 SER A 192  THR A 198 -1  O  THR A 194   N  LYS A 150           
SHEET    4   F 4 ILE A 206  ASN A 211 -1  O  PHE A 210   N  TYR A 193           
SHEET    1   G 5 THR B  58  TYR B  60  0                                        
SHEET    2   G 5 LEU B  46  ASN B  53 -1  N  TYR B  51   O  SER B  59           
SHEET    3   G 5 ALA B  34  GLN B  40 -1  N  ARG B  39   O  GLU B  47           
SHEET    4   G 5 ALA B  92  GLY B  99 -1  O  GLY B  99   N  ALA B  34           
SHEET    5   G 5 MET B 105  TRP B 108 -1  O  ASP B 106   N  ARG B  98           
SHEET    1   H 6 THR B  58  TYR B  60  0                                        
SHEET    2   H 6 LEU B  46  ASN B  53 -1  N  TYR B  51   O  SER B  59           
SHEET    3   H 6 ALA B  34  GLN B  40 -1  N  ARG B  39   O  GLU B  47           
SHEET    4   H 6 ALA B  92  GLY B  99 -1  O  GLY B  99   N  ALA B  34           
SHEET    5   H 6 ALA B 112  VAL B 116 -1  O  ALA B 112   N  TYR B  94           
SHEET    6   H 6 LEU B  11  VAL B  12  1  N  VAL B  12   O  THR B 115           
SHEET    1   I 3 LEU B  18  THR B  23  0                                        
SHEET    2   I 3 GLN B  78  LEU B  83 -1  O  PHE B  79   N  CYS B  22           
SHEET    3   I 3 THR B  71  ASP B  73 -1  N  ASP B  73   O  GLN B  78           
SHEET    1   J 4 SER B 125  LEU B 129  0                                        
SHEET    2   J 4 SER B 140  TYR B 150 -1  O  GLY B 144   N  LEU B 129           
SHEET    3   J 4 TYR B 180  THR B 189 -1  O  LEU B 182   N  VAL B 147           
SHEET    4   J 4 VAL B 168  THR B 170 -1  N  HIS B 169   O  SER B 185           
SHEET    1   K 4 SER B 125  LEU B 129  0                                        
SHEET    2   K 4 SER B 140  TYR B 150 -1  O  GLY B 144   N  LEU B 129           
SHEET    3   K 4 TYR B 180  THR B 189 -1  O  LEU B 182   N  VAL B 147           
SHEET    4   K 4 LEU B 174  LEU B 175 -1  N  LEU B 174   O  THR B 181           
SHEET    1   L 3 THR B 156  TRP B 159  0                                        
SHEET    2   L 3 THR B 199  HIS B 204 -1  O  ALA B 203   N  THR B 156           
SHEET    3   L 3 THR B 209  LYS B 214 -1  O  THR B 209   N  HIS B 204           
SSBOND   1 CYS A   23    CYS A   89                          1555   1555  2.04  
SSBOND   2 CYS A  135    CYS A  195                          1555   1555  2.05  
SSBOND   3 CYS B   22    CYS B   96                          1555   1555  2.05  
SSBOND   4 CYS B  145    CYS B  200                          1555   1555  2.04  
LINK        CD    CD A 216                 NH1 ARG A  62     1555   1555  2.18  
LINK        CD    CD A 216                 NH2 ARG A  62     1555   1555  2.55  
LINK        CD    CD A 216                 OE1 GLU A  82     1555   1555  2.78  
LINK        CD    CD A 216                 OE2 GLU A  82     1555   1555  3.10  
LINK        CD    CD A 217                 OD1 ASP A 168     1555   1555  2.63  
LINK        CD    CD A 218                 OE2 GLU A  17     1555   1555  2.63  
LINK        CD    CD B 220                 OD2 ASP B 178     1555   1555  2.12  
LINK        CD    CD B 220                 OD1 ASP B 178     1555   1555  1.91  
LINK         K     K C   1                 O   TYR C 199     1555   1555  2.88  
LINK         K     K C   1                 K     K C   2     1555   1555  3.40  
LINK         K     K C   2                 O   GLY C 198     1555   1555  2.85  
LINK         K     K C   2                 K     K C   3     1555   1555  3.21  
LINK         K     K C   2                 O   VAL C 197     1555   1555  3.35  
LINK         K     K C   3                 O   VAL C 197     1555   1555  3.05  
LINK         K     K C   3                 K     K C   4     1555   1555  3.34  
LINK         K     K C   3                 O   THR C 196     1555   1555  2.95  
LINK         K     K C   4                 OG1 THR C 196     1555   1555  2.83  
LINK         K     K C   4                 O   THR C 196     1555   1555  2.53  
LINK        CD    CD C   7                 OD1 ASP C 185     1555   1555  2.33  
LINK        CD    CD C   7                 OD2 ASP C 185     1555   1555  2.70  
LINK        CD    CD C   9                 NH1 ARG C 133     1555   1555  2.69  
LINK        CD    CD C   9                 NH2 ARG C 133     1555   1555  2.71  
LINK        CD    CD C   9                 NE  ARG C 133     1555   1555  2.95  
LINK        CD    CD A 216                 NH1 ARG A  62     1555   5755  2.18  
LINK        CD    CD A 216                 NH2 ARG A  62     1555   5755  2.55  
LINK        CD    CD A 216                 OE1 GLU A  82     1555   5755  2.78  
LINK        CD    CD A 216                 OE2 GLU A  82     1555   5755  3.10  
LINK        CD    CD B 220                 OD2 ASP A 152     1555  15545  1.99  
LINK        CD    CD B 220                 ND1 HIS A 190     1555  15545  2.21  
LINK         K     K C   1                 O   TYR C 199     1555   4665  2.88  
LINK         K     K C   1                 O   TYR C 199     1555   3645  2.88  
LINK         K     K C   1                 O   TYR C 199     1555   2755  2.88  
LINK         K     K C   1                 K     K C   2     1555   2755  3.40  
LINK         K     K C   1                 K     K C   2     1555   3645  3.40  
LINK         K     K C   1                 K     K C   2     1555   4665  3.40  
LINK         K     K C   2                 K     K C   3     1555   4665  3.21  
LINK         K     K C   2                 K     K C   3     1555   3645  3.21  
LINK         K     K C   2                 K     K C   3     1555   2755  3.21  
LINK         K     K C   2                 O   GLY C 198     1555   4665  2.85  
LINK         K     K C   2                 O   VAL C 197     1555   2755  3.35  
LINK         K     K C   2                 O   GLY C 198     1555   3645  2.85  
LINK         K     K C   2                 O   GLY C 198     1555   2755  2.85  
LINK         K     K C   2                 O   VAL C 197     1555   4665  3.35  
LINK         K     K C   2                 O   VAL C 197     1555   3645  3.35  
LINK         K     K C   3                 O   VAL C 197     1555   4665  3.05  
LINK         K     K C   3                 O   VAL C 197     1555   3645  3.05  
LINK         K     K C   3                 O   VAL C 197     1555   2755  3.05  
LINK         K     K C   3                 K     K C   4     1555   4665  3.34  
LINK         K     K C   3                 K     K C   4     1555   3645  3.34  
LINK         K     K C   3                 K     K C   4     1555   2755  3.34  
LINK         K     K C   3                 O   THR C 196     1555   4665  2.95  
LINK         K     K C   3                 O   THR C 196     1555   3645  2.95  
LINK         K     K C   3                 O   THR C 196     1555   2755  2.95  
LINK         K     K C   4                 OG1 THR C 196     1555   4665  2.83  
LINK         K     K C   4                 OG1 THR C 196     1555   3645  2.83  
LINK         K     K C   4                 OG1 THR C 196     1555   2755  2.83  
LINK         K     K C   4                 O   THR C 196     1555   4665  2.53  
LINK         K     K C   4                 O   THR C 196     1555   3645  2.53  
LINK         K     K C   4                 O   THR C 196     1555   2755  2.53  
CISPEP   1 SER A    7    PRO A    8          0        -0.24                     
CISPEP   2 TYR A  141    PRO A  142          0        -0.11                     
CISPEP   3 PHE B  151    PRO B  152          0         0.00                     
CISPEP   4 GLU B  153    PRO B  154          0         0.57                     
CISPEP   5 TRP B  193    PRO B  194          0         0.04                     
SITE     1 AC1  2   K C   2  TYR C 199                                          
SITE     1 AC2  4   K C   1    K C   3  VAL C 197  GLY C 198                    
SITE     1 AC3  4   K C   2    K C   4  THR C 196  VAL C 197                    
SITE     1 AC4  2   K C   3  THR C 196                                          
SITE     1 AC5  2 SER C 182  ASP C 185                                          
SITE     1 AC6  1 CYS C  46                                                     
SITE     1 AC7  2 PRO C  95  ARG C 133                                          
SITE     1 AC8  2 ARG A  62  GLU A  82                                          
SITE     1 AC9  1 ASP A 168                                                     
SITE     1 BC1  3 ASP A 152  HIS A 190  ASP B 178                               
SITE     1 BC2  1 GLU A  17                                                     
CRYST1  189.439  189.439  150.479  90.00  90.00  90.00 I 4 2 2      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      0.005279  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005279  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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