GenomeNet

Database: PDB
Entry: 3F7V
LinkDB: 3F7V
Original site: 3F7V 
HEADER    MEMBRANE PROTEIN/METAL TRANSPORT        10-NOV-08   3F7V              
TITLE     KCSA POTASSIUM CHANNEL IN THE OPEN-INACTIVATED STATE WITH 23 A OPENING
TITLE    2 AT T112                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN;                         
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;                           
COMPND   9 CHAIN: C;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_TAXID: 10090;                                               
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   6 ORGANISM_TAXID: 10090;                                               
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;                          
SOURCE   9 ORGANISM_TAXID: 1916;                                                
SOURCE  10 GENE: KCSA, SKC1;                                                    
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: XL10-GOLD;                                 
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_VECTOR: PQE70                                      
KEYWDS    KCSA, POTASSIUM CHANNEL, INACTIVATION, OPEN, CELL MEMBRANE, ION       
KEYWDS   2 TRANSPORT, IONIC CHANNEL, MEMBRANE, TRANSMEMBRANE, TRANSPORT,        
KEYWDS   3 VOLTAGE-GATED CHANNEL, MEMBRANE PROTEIN-METAL TRANSPORT COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.G.CUELLO,V.JOGINI,D.M.CORTES,E.PEROZO                               
REVDAT   4   27-DEC-23 3F7V    1       REMARK                                   
REVDAT   3   20-OCT-21 3F7V    1       REMARK SEQADV LINK                       
REVDAT   2   09-FEB-11 3F7V    1       REMARK                                   
REVDAT   1   19-MAY-10 3F7V    0                                                
JRNL        AUTH   L.G.CUELLO,V.JOGINI,D.M.CORTES,E.PEROZO                      
JRNL        TITL   KCSA POTASSIUM CHANNEL IN THE OPEN-INACTIVATED STATE WITH 23 
JRNL        TITL 2 A OPENING AT T112                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 13848                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1297                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3938                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.413                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3F7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0-6.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13848                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG400, 50MM MAGNESIUM ACETATE,   
REMARK 280  50MM SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
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+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   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       77.97450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.97450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       36.70900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       77.97450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.97450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       36.70900            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       77.97450            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       77.97450            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       36.70900            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       77.97450            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       77.97450            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       36.70900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
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      311.89800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -311.89800            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000     -311.89800            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      311.89800            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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 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     GLY C    21                                                      
REMARK 465     SER C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     GLN C    25                                                      
REMARK 465     TRP C    26                                                      
REMARK 465     ARG C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     GLN C   119                                                      
REMARK 465     GLN C   120                                                      
REMARK 465     GLN C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     GLN C   124                                                      
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     TYR C  45    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C  49    CG   CD1  CD2                                       
REMARK 470     VAL C  95    CG1  CG2                                            
REMARK 470     GLN C 117    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 118    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 145   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
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    GLU A  10      116.49   -161.62                                   
REMARK 500    CYS A  22      104.86   -170.34                                   
REMARK 500    SER A  54       26.59    -74.09                                   
REMARK 500    TYR A  55      -36.90   -168.49                                   
REMARK 500    LYS A  74      -56.16    -27.22                                   
REMARK 500    SER A  85       77.99     40.79                                   
REMARK 500    ALA A  92     -177.02    177.20                                   
REMARK 500    ARG A 100       26.59    -75.69                                   
REMARK 500    ALA A 119      166.07    -47.60                                   
REMARK 500    LEU A 129       89.07   -151.20                                   
REMARK 500    SER A 133      -36.01    -36.29                                   
REMARK 500    ASN A 138     -165.30   -125.02                                   
REMARK 500    CYS A 145      130.86   -174.66                                   
REMARK 500    PRO A 154     -169.87   -108.74                                   
REMARK 500    SER A 192       -2.34    -53.34                                   
REMARK 500    PRO B  15      160.24    -48.25                                   
REMARK 500    ASP B  32       45.38    -76.22                                   
REMARK 500    ALA B  51      -40.28     75.39                                   
REMARK 500    SER B  77       76.24     73.38                                   
REMARK 500    SER B  80      -45.82    -29.22                                   
REMARK 500    ALA B  84     -164.00   -166.94                                   
REMARK 500    PHE B  96      150.40    -46.73                                   
REMARK 500    ARG B 108     -169.99   -106.51                                   
REMARK 500    THR B 126       -6.46    -56.94                                   
REMARK 500    TYR B 140      132.94   -176.29                                   
REMARK 500    PRO B 141      173.00    -54.40                                   
REMARK 500    ASP B 170       19.73   -142.80                                   
REMARK 500    THR B 172     -164.06   -108.78                                   
REMARK 500    ASP B 184      -70.98    -49.33                                   
REMARK 500    ASN B 190      -84.72    -66.85                                   
REMARK 500    LYS B 199      -15.10    -35.85                                   
REMARK 500    PHE B 209      137.98   -175.60                                   
REMARK 500    THR C  33        0.39    -53.55                                   
REMARK 500    SER C  69      -75.71    -56.92                                   
REMARK 500    TRP C 113      -19.41    -42.78                                   
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                               K C   2   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  75   O                                                      
REMARK 620 2 THR C  75   OG1  46.2                                              
REMARK 620 N                    1                                               
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 2                     
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FB5   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT 2.8A RESOLUTION                                      
REMARK 900 RELATED ID: 3FB6   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT 3.0A RESOLUTION                                      
REMARK 900 RELATED ID: 3FB7   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT 3.3A RESOLUTION                                      
REMARK 900 RELATED ID: 3FB8   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT 3.4A RESOLUTION                                      
REMARK 900 RELATED ID: 3F7Y   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT 3.4A RESOLUTION                                      
DBREF  3F7V C   21   124  UNP    P0A334   KCSA_STRLI      21    124             
DBREF  3F7V A    1   219  PDB    3F7V     3F7V             1    219             
DBREF  3F7V B    1   212  PDB    3F7V     3F7V             1    212             
SEQADV 3F7V GLN C   25  UNP  P0A334    HIS    25 ENGINEERED MUTATION            
SEQADV 3F7V CYS C   90  UNP  P0A334    LEU    90 ENGINEERED MUTATION            
SEQADV 3F7V GLN C  117  UNP  P0A334    ARG   117 ENGINEERED MUTATION            
SEQADV 3F7V GLN C  120  UNP  P0A334    GLU   120 ENGINEERED MUTATION            
SEQADV 3F7V GLN C  121  UNP  P0A334    ARG   121 ENGINEERED MUTATION            
SEQADV 3F7V GLN C  122  UNP  P0A334    ARG   122 ENGINEERED MUTATION            
SEQADV 3F7V GLN C  124  UNP  P0A334    HIS   124 ENGINEERED MUTATION            
SEQRES   1 A  219  GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS          
SEQRES   2 A  219  PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY          
SEQRES   3 A  219  TYR THR PHE THR SER ASP TRP ILE HIS TRP VAL LYS GLN          
SEQRES   4 A  219  ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE ILE          
SEQRES   5 A  219  PRO SER TYR GLY ARG ALA ASN TYR ASN GLU LYS ILE GLN          
SEQRES   6 A  219  LYS LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR          
SEQRES   7 A  219  ALA PHE MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 A  219  ALA VAL TYR TYR CYS ALA ARG GLU ARG GLY ASP GLY TYR          
SEQRES   9 A  219  PHE ALA VAL TRP GLY ALA GLY THR THR VAL THR VAL SER          
SEQRES  10 A  219  SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 A  219  PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU          
SEQRES  12 A  219  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 A  219  VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS          
SEQRES  14 A  219  THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 A  219  SER SER SER VAL THR VAL PRO SER SER SER TRP PRO SER          
SEQRES  16 A  219  GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 A  219  THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP                  
SEQRES   1 B  212  ASP ILE LEU LEU THR GLN SER PRO ALA ILE LEU SER VAL          
SEQRES   2 B  212  SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER          
SEQRES   3 B  212  GLN SER ILE GLY THR ASP ILE HIS TRP TYR GLN GLN ARG          
SEQRES   4 B  212  THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER          
SEQRES   5 B  212  GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 B  212  GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL          
SEQRES   7 B  212  GLU SER GLU ASP ILE ALA ASN TYR TYR CYS GLN GLN SER          
SEQRES   8 B  212  ASN ARG TRP PRO PHE THR PHE GLY SER GLY THR LYS LEU          
SEQRES   9 B  212  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 B  212  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 B  212  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 B  212  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 B  212  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 B  212  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 B  212  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 B  212  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 B  212  PHE ASN ARG ASN                                              
SEQRES   1 C  104  GLY SER ALA LEU GLN TRP ARG ALA ALA GLY ALA ALA THR          
SEQRES   2 C  104  VAL LEU LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU          
SEQRES   3 C  104  ALA VAL LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU          
SEQRES   4 C  104  ILE THR TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR          
SEQRES   5 C  104  ALA THR THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR          
SEQRES   6 C  104  LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA          
SEQRES   7 C  104  GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA          
SEQRES   8 C  104  THR TRP PHE VAL GLY GLN GLU GLN GLN GLN GLN GLY GLN          
HET      K  C   1       1                                                       
HET      K  C   2       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   4    K    2(K 1+)                                                      
HELIX    1   1 THR A   87  SER A   91  5                                   5    
HELIX    2   2 PRO A  205  SER A  208  5                                   4    
HELIX    3   3 GLU B   79  ILE B   83  5                                   5    
HELIX    4   4 SER B  121  THR B  126  1                                   6    
HELIX    5   5 LYS B  183  ARG B  188  1                                   6    
HELIX    6   6 ALA C   31  ARG C   52  1                                  22    
HELIX    7   7 THR C   61  THR C   75  1                                  15    
HELIX    8   8 TRP C   87  GLU C  118  1                                  32    
SHEET    1   A 6 ALA A   9  VAL A  12  0                                        
SHEET    2   A 6 THR A 112  VAL A 116  1  O  THR A 115   N  VAL A  12           
SHEET    3   A 6 ALA A  92  GLU A  99 -1  N  ALA A  92   O  VAL A 114           
SHEET    4   A 6 TRP A  33  GLN A  39 -1  N  VAL A  37   O  TYR A  95           
SHEET    5   A 6 GLU A  46  ILE A  51 -1  O  GLU A  46   N  LYS A  38           
SHEET    6   A 6 ALA A  58  TYR A  60 -1  O  ASN A  59   N  GLU A  50           
SHEET    1   B 4 ALA A   9  VAL A  12  0                                        
SHEET    2   B 4 THR A 112  VAL A 116  1  O  THR A 115   N  VAL A  12           
SHEET    3   B 4 ALA A  92  GLU A  99 -1  N  ALA A  92   O  VAL A 114           
SHEET    4   B 4 PHE A 105  TRP A 108 -1  O  VAL A 107   N  ARG A  98           
SHEET    1   C 3 VAL A  18  LYS A  23  0                                        
SHEET    2   C 3 THR A  78  LEU A  83 -1  O  LEU A  83   N  VAL A  18           
SHEET    3   C 3 ALA A  68  ASP A  73 -1  N  THR A  71   O  PHE A  80           
SHEET    1   D 4 SER A 125  LEU A 129  0                                        
SHEET    2   D 4 MET A 140  TYR A 150 -1  O  LYS A 148   N  SER A 125           
SHEET    3   D 4 LEU A 179  PRO A 189 -1  O  TYR A 180   N  TYR A 150           
SHEET    4   D 4 VAL A 168  THR A 170 -1  N  HIS A 169   O  SER A 185           
SHEET    1   E 4 SER A 125  LEU A 129  0                                        
SHEET    2   E 4 MET A 140  TYR A 150 -1  O  LYS A 148   N  SER A 125           
SHEET    3   E 4 LEU A 179  PRO A 189 -1  O  TYR A 180   N  TYR A 150           
SHEET    4   E 4 VAL A 174  GLN A 176 -1  N  VAL A 174   O  THR A 181           
SHEET    1   F 3 THR A 156  TRP A 159  0                                        
SHEET    2   F 3 CYS A 200  HIS A 204 -1  O  ASN A 201   N  THR A 158           
SHEET    3   F 3 THR A 209  VAL A 211 -1  O  VAL A 211   N  VAL A 202           
SHEET    1   G 4 LEU B   4  GLN B   6  0                                        
SHEET    2   G 4 ARG B  18  ALA B  25 -1  O  ARG B  24   N  THR B   5           
SHEET    3   G 4 ASP B  70  ASN B  76 -1  O  PHE B  71   N  CYS B  23           
SHEET    4   G 4 PHE B  62  SER B  67 -1  N  SER B  63   O  SER B  74           
SHEET    1   H 5 ILE B  10  VAL B  13  0                                        
SHEET    2   H 5 THR B 102  ILE B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3   H 5 ASN B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   H 5 ILE B  33  GLN B  38 -1  N  HIS B  34   O  GLN B  89           
SHEET    5   H 5 ARG B  45  ILE B  48 -1  O  LEU B  47   N  TRP B  35           
SHEET    1   I 4 ILE B  10  VAL B  13  0                                        
SHEET    2   I 4 THR B 102  ILE B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3   I 4 ASN B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   I 4 THR B  97  PHE B  98 -1  O  THR B  97   N  GLN B  90           
SHEET    1   J 4 THR B 114  PHE B 118  0                                        
SHEET    2   J 4 GLY B 129  PHE B 139 -1  O  VAL B 133   N  PHE B 118           
SHEET    3   J 4 TYR B 173  THR B 182 -1  O  LEU B 181   N  ALA B 130           
SHEET    4   J 4 VAL B 159  LEU B 160 -1  N  LEU B 160   O  THR B 178           
SHEET    1   K 4 SER B 153  ARG B 155  0                                        
SHEET    2   K 4 ASN B 145  ILE B 150 -1  N  TRP B 148   O  ARG B 155           
SHEET    3   K 4 SER B 191  HIS B 198 -1  O  GLU B 195   N  LYS B 147           
SHEET    4   K 4 SER B 201  ASN B 210 -1  O  SER B 201   N  HIS B 198           
SSBOND   1 CYS A   22    CYS A   96                          1555   1555  2.05  
SSBOND   2 CYS A  145    CYS A  200                          1555   1555  2.07  
SSBOND   3 CYS B   23    CYS B   88                          1555   1555  2.04  
SSBOND   4 CYS B  134    CYS B  194                          1555   1555  2.03  
LINK         K     K C   2                 O   THR C  75     1555   1555  3.22  
LINK         K     K C   2                 OG1 THR C  75     1555   1555  3.28  
CISPEP   1 PHE A  151    PRO A  152          0        -0.13                     
CISPEP   2 GLU A  153    PRO A  154          0         0.18                     
CISPEP   3 TRP A  193    PRO A  194          0        -1.26                     
CISPEP   4 SER B    7    PRO B    8          0        -0.06                     
CISPEP   5 TRP B   94    PRO B   95          0        -2.18                     
CISPEP   6 TYR B  140    PRO B  141          0         0.09                     
SITE     1 AC1  1 THR C  75                                                     
CRYST1  155.949  155.949   73.418  90.00  90.00  90.00 I 4           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006412  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006412  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013621        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system