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Database: PDB
Entry: 2A0L
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Original site: 2A0L 
HEADER    MEMBRANE PROTEIN                        16-JUN-05   2A0L              
TITLE     CRYSTAL STRUCTURE OF KVAP-33H1 FV COMPLEX                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KVAP K+ CHANNEL;                                           
COMPND   5 SYNONYM: KVAP;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 33H1 FV FRAGMENT;                                          
COMPND   9 CHAIN: C, E;                                                         
COMPND  10 FRAGMENT: FV FRAGMENT,LIGHT CHAIN;                                   
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: 33H1 FV FRAGMENT;                                          
COMPND  13 CHAIN: D, F;                                                         
COMPND  14 FRAGMENT: FV FRAGMENT, HEAVY CHAIN                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 56636;                                               
SOURCE   4 GENE: KVAP_AERPE;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: XL1BLUE;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 OTHER_DETAILS: MOUSE HYBRIDOMA;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 OTHER_DETAILS: MOUSE HYBRIDOMA                                       
KEYWDS    VOLTAGE SENSOR, VOLTAGE-DEPENDENT K+ CHANNEL, K+ CHANNEL-FV           
KEYWDS   2 COMPLEX, MEMBRANE PROTEIN, ION CHANNEL                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.Y.LEE,A.LEE,J.CHEN,R.MACKINNON                                      
REVDAT   2   24-FEB-09 2A0L    1       VERSN                                    
REVDAT   1   01-NOV-05 2A0L    0                                                
JRNL        AUTH   S.Y.LEE,A.LEE,J.CHEN,R.MACKINNON                             
JRNL        TITL   STRUCTURE OF THE KVAP VOLTAGE-DEPENDENT K+ CHANNEL           
JRNL        TITL 2 AND ITS DEPENDENCE ON THE LIPID MEMBRANE.                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102 15441 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16223877                                                     
JRNL        DOI    10.1073/PNAS.0507651102                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 3.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 6294012.310                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 16234                          
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) : 0.358                           
REMARK   3   FREE R VALUE                     : 0.392                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 789                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.014                           
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) : 3.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.14                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2586                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4380                       
REMARK   3   BIN FREE R VALUE                    : 0.4370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 117                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.040                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6742                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
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) : 187.80                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 34.47000                                             
REMARK   3    B22 (A**2) : 34.47000                                             
REMARK   3    B33 (A**2) : -68.95000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.81                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.90                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.88                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.98                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
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) : 18.010; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 27.940; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 18.270; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 26.670; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.26                                                 
REMARK   3   BSOL        : 164.24                                               
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 2A0L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033341.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-04; 18-NOV-04; 07-DEC-      
REMARK 200                                   04                                 
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100; 100                      
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y                            
REMARK 200  RADIATION SOURCE               : NSLS; ALS; CHESS                   
REMARK 200  BEAMLINE                       : X25; 8.2.1; A1                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1; 1.1; 0.9795                   
REMARK 200  MONOCHROMATOR                  : SI(111); NULL; NULL                
REMARK 200  OPTICS                         : NULL; NULL; NULL                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; CCD                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC             
REMARK 200                                   QUANTUM 210; ADSC Q210             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16257                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.940                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL                  
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, TRIC-HCL, PH 8.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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+1/2                                              
REMARK 290       4555   Y,-X,Z+1/2                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z+1/2                                              
REMARK 290       8555   -Y,-X,-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       95.90600            
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       95.90600            
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       95.90600            
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       95.90600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM THE     
REMARK 300 DIMER IN THE ASYMMETRIC UNIT BY THE OPERATION : X. -Y+1,-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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      136.36200            
REMARK 350   BIOMT3   2  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 B   1  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A   2  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A   3  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K B   4  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     LEU A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     ILE A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     VAL A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     PRO A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     ILE B   238                                                      
REMARK 465     LEU B   239                                                      
REMARK 465     VAL B   240                                                      
REMARK 465     GLY B   241                                                      
REMARK 465     GLU B   242                                                      
REMARK 465     PRO B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     PRO B   245                                                      
REMARK 465     SER B   246                                                      
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    GLN A  49        5.98    -61.29                                   
REMARK 500    LEU A  55      -94.80    -86.60                                   
REMARK 500    VAL A  56      -35.46    -32.27                                   
REMARK 500    ALA A  77      170.08    -44.38                                   
REMARK 500    TYR A  78       57.69    -69.96                                   
REMARK 500    LYS A  79       -6.39   -152.86                                   
REMARK 500    VAL A  87      -45.46    174.91                                   
REMARK 500    LEU A  97       36.88    -84.61                                   
REMARK 500    VAL A  98      -73.20   -102.00                                   
REMARK 500    PRO A  99      -90.65   -142.22                                   
REMARK 500    ALA A 100      -69.29    158.52                                   
REMARK 500    LEU A 102        4.91    -65.69                                   
REMARK 500    LEU A 110      -61.23    -95.41                                   
REMARK 500    LEU A 113       33.50    -98.01                                   
REMARK 500    LEU A 115       35.32    -71.12                                   
REMARK 500    SER A 132      -73.06    -61.03                                   
REMARK 500    ILE A 141      173.50    -24.26                                   
REMARK 500    ALA A 142       -3.90     87.80                                   
REMARK 500    ILE A 148      -46.13    175.65                                   
REMARK 500    PHE A 150      -79.68    -61.74                                   
REMARK 500    GLU A 172      -37.24   -131.75                                   
REMARK 500    PRO A 176     -100.46    -59.11                                   
REMARK 500    SER A 179      -16.70    -46.02                                   
REMARK 500    LYS A 181      -84.62   -132.89                                   
REMARK 500    SER A 182      172.59    -59.63                                   
REMARK 500    TYR A 199     -141.26   -114.84                                   
REMARK 500    VAL A 211      -74.86    -58.28                                   
REMARK 500    THR A 219      -74.56    -98.47                                   
REMARK 500    ILE A 221      -72.09    -58.51                                   
REMARK 500    GLN A 236       34.07    -81.65                                   
REMARK 500    GLN B  49        5.45    -61.40                                   
REMARK 500    TYR B  54       -9.02    -50.83                                   
REMARK 500    LEU B  55      -94.80    -89.63                                   
REMARK 500    VAL B  56      -35.50    -32.25                                   
REMARK 500    ALA B  77      169.65    -43.06                                   
REMARK 500    LYS B  79      -10.04   -154.73                                   
REMARK 500    VAL B  87      -44.88    178.65                                   
REMARK 500    LEU B  97       29.86    -69.12                                   
REMARK 500    VAL B  98      -76.74    -96.17                                   
REMARK 500    PRO B  99      -96.12   -144.31                                   
REMARK 500    ALA B 100      -67.41    164.80                                   
REMARK 500    LEU B 102        4.63    -65.24                                   
REMARK 500    LEU B 110      -61.18    -95.46                                   
REMARK 500    LEU B 113       33.71    -98.06                                   
REMARK 500    LEU B 115       35.04    -71.03                                   
REMARK 500    SER B 132      -73.01    -61.04                                   
REMARK 500    LEU B 138        6.53    -68.48                                   
REMARK 500    ALA B 142      -17.66    -45.57                                   
REMARK 500    LYS B 147       66.70    -68.95                                   
REMARK 500    ILE B 148      -46.19    177.20                                   
REMARK 500    PHE B 150      -79.84    -61.69                                   
REMARK 500    GLU B 172      -37.23   -131.73                                   
REMARK 500    PRO B 176     -100.39    -59.11                                   
REMARK 500    SER B 179      -16.67    -46.14                                   
REMARK 500    LYS B 181      -84.72   -132.86                                   
REMARK 500    SER B 182      172.65    -59.60                                   
REMARK 500    TYR B 199     -141.27   -114.93                                   
REMARK 500    VAL B 211      -74.85    -58.23                                   
REMARK 500    THR B 219      -74.54    -98.58                                   
REMARK 500    ILE B 221      -72.03    -58.59                                   
REMARK 500    ALA C  13     -177.13    160.98                                   
REMARK 500    LEU C  15      117.01    -13.31                                   
REMARK 500    SER C  28      174.28    -54.12                                   
REMARK 500    VAL C  29     -131.69   -141.54                                   
REMARK 500    SER C  30      105.99   -168.52                                   
REMARK 500    SER C  31      -29.38    -33.06                                   
REMARK 500    TYR C  33       17.65    -63.08                                   
REMARK 500    PRO C  41      128.55    -38.00                                   
REMARK 500    SER C  43     -157.84    -85.70                                   
REMARK 500    THR C  52      -56.64     65.54                                   
REMARK 500    SER C  68      142.71    174.95                                   
REMARK 500    THR C  75      146.61    -23.61                                   
REMARK 500    ILE C  76     -135.88   -126.33                                   
REMARK 500    SER C  77      -33.26   -162.42                                   
REMARK 500    GLU C  80     -153.56   -150.06                                   
REMARK 500    ASP C  83      -14.87    -46.03                                   
REMARK 500    ALA C  84       75.38    -65.02                                   
REMARK 500    HIS C  93      -84.58   -107.17                                   
REMARK 500    SER C  95     -153.90   -128.39                                   
REMARK 500    GLN D   3      125.25    177.33                                   
REMARK 500    PRO D   9     -107.82    -56.57                                   
REMARK 500    LEU D  11      125.92    169.24                                   
REMARK 500    SER D  15       -9.60     76.18                                   
REMARK 500    TYR D  27     -162.77   -161.05                                   
REMARK 500    ASN D  31      -93.77    -55.90                                   
REMARK 500    TYR D  33     -178.95     71.84                                   
REMARK 500    ASN D  44        8.33     55.32                                   
REMARK 500    THR D  57      154.63    -43.13                                   
REMARK 500    PRO D  62      -18.93    -44.13                                   
REMARK 500    ASP D  73       75.80   -102.99                                   
REMARK 500    THR D  74      -36.13    -37.44                                   
REMARK 500    ASN D  77       70.20     73.56                                   
REMARK 500    SER D  85       72.07     59.40                                   
REMARK 500    ALA D  92     -164.66   -176.66                                   
REMARK 500    ASP D 101      147.56    -30.44                                   
REMARK 500    TYR D 102       20.25     42.09                                   
REMARK 500    PHE D 103      102.64     68.44                                   
REMARK 500    ALA D 104       88.90   -172.00                                   
REMARK 500    MET D 105      104.07    -43.95                                   
REMARK 500    ALA E  13     -169.12    174.98                                   
REMARK 500    SER E  28      174.34    -52.39                                   
REMARK 500    VAL E  29     -131.95   -142.86                                   
REMARK 500    SER E  30      108.25   -166.37                                   
REMARK 500    SER E  31      -25.90    -35.77                                   
REMARK 500    TYR E  33       17.75    -61.63                                   
REMARK 500    PRO E  41      127.22    -36.03                                   
REMARK 500    SER E  43     -159.74    -84.12                                   
REMARK 500    TRP E  48      -37.57   -132.73                                   
REMARK 500    THR E  52      -57.18     69.04                                   
REMARK 500    ALA E  61      -11.77    -48.37                                   
REMARK 500    SER E  68      144.16    170.66                                   
REMARK 500    THR E  75      145.91    -21.84                                   
REMARK 500    ILE E  76     -137.50   -125.76                                   
REMARK 500    SER E  77      -31.22   -162.07                                   
REMARK 500    GLU E  80     -151.30   -157.83                                   
REMARK 500    ASP E  83      -14.08    -46.01                                   
REMARK 500    ALA E  84       76.79    -67.01                                   
REMARK 500    HIS E  93      -90.59   -102.70                                   
REMARK 500    SER E  95     -153.66   -130.26                                   
REMARK 500    PRO F   9     -106.28    -72.92                                   
REMARK 500    LEU F  11      126.45    167.28                                   
REMARK 500    PRO F  14      152.42    -46.91                                   
REMARK 500    SER F  15      -16.41     75.31                                   
REMARK 500    TYR F  27     -162.84   -160.93                                   
REMARK 500    ASN F  31      -94.00    -56.00                                   
REMARK 500    TYR F  33     -179.07     71.71                                   
REMARK 500    ASN F  44        8.28     55.64                                   
REMARK 500    THR F  57      154.60    -43.15                                   
REMARK 500    PRO F  62      -19.00    -44.21                                   
REMARK 500    ASP F  73       75.52   -103.38                                   
REMARK 500    THR F  74      -35.70    -37.27                                   
REMARK 500    ASN F  77       70.52     73.28                                   
REMARK 500    SER F  85       72.33     59.31                                   
REMARK 500    ALA F  92     -164.55   -176.57                                   
REMARK 500    ASP F 101      147.51    -30.15                                   
REMARK 500    TYR F 102       20.05     42.15                                   
REMARK 500    PHE F 103      102.72     68.56                                   
REMARK 500    ALA F 104       89.29   -172.04                                   
REMARK 500    MET F 105      103.55    -44.42                                   
REMARK 500    TYR F 107      118.23   -166.13                                   
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 A   2   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL B 197   O                                                      
REMARK 620 2   K A   3   K    60.7                                              
REMARK 620 3 VAL A 197   O    76.5  62.7                                        
REMARK 620 4 GLY B 198   O    42.2 102.9  97.1                                  
REMARK 620 5   K B   1   K   119.3 180.0 117.3  77.1                            
REMARK 620 6 GLY A 198   O    94.5 104.2  41.5  86.3  75.8                      
REMARK 620 7 VAL A 197   O    77.6  62.7 125.5  94.6 117.3 166.8                
REMARK 620 8 VAL B 197   O   121.5  60.7  77.6 163.5 119.3  99.3  76.5          
REMARK 620 9   K A   3   K    60.7   0.0  62.7 102.9 180.0 104.2  62.7  60.7    
REMARK 620 10 GLY A 198   O    99.3 104.2 166.8  87.5  75.8 151.6  41.5         
REMARK 620  94.5 104.2                                                          
REMARK 620 11 GLY B 198   O   163.5 102.9  94.6 154.2  77.1  87.5  97.1         
REMARK 620  42.2 102.9  86.3                                                    
REMARK 620 12   K B   1   K   119.3 180.0 117.3  77.1   0.0  75.8 117.3         
REMARK 620  119.3 180.0  75.8  77.1                                             
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620     9     10     11                                                  
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A   3   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 197   O                                                      
REMARK 620 2 THR A 196   O    62.9                                              
REMARK 620 3   K B   4   K   120.8  60.5                                        
REMARK 620 4 THR B 196   O   120.6  75.1  58.2                                  
REMARK 620 5 VAL B 197   O    74.6  89.7 120.1  64.7                            
REMARK 620 6   K B   4   K   120.8  60.5   0.0  58.2 120.1                      
REMARK 620 7 THR A 196   O   163.6 121.1  60.5  74.8 120.0  60.5                
REMARK 620 8 VAL A 197   O   118.5 163.6 120.8  91.7  75.6 120.8  62.9          
REMARK 620 9 THR B 196   O    91.7  74.8  58.2 116.5 163.0  58.2  75.1 120.6    
REMARK 620 10 VAL B 197   O    75.6 120.0 120.1 163.0 119.7 120.1  89.7         
REMARK 620  74.6  64.7                                                          
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620     9                                                                
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B   1   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 199   O                                                      
REMARK 620 2 TYR B 199   O    88.3                                              
REMARK 620 3 TYR B 199   O    88.5 162.0                                        
REMARK 620 4 TYR A 199   O   159.6  88.5  88.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B   4   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 196   OG1                                                    
REMARK 620 2 THR B 196   O   115.3                                              
REMARK 620 3 THR A 196   O    53.0  72.8                                        
REMARK 620 4 THR B 196   OG1  84.5  55.0  84.4                                  
REMARK 620 5 THR A 196   OG1 147.0  83.2 155.7  85.2                            
REMARK 620 6 THR B 196   OG1  85.2 156.9 116.4 143.0  84.5                      
REMARK 620 7 THR A 196   O   155.7  72.5 113.7 116.4  53.0  84.4                
REMARK 620 8 THR B 196   O    83.2 114.0  72.5 156.9 115.3  55.0  72.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1                     
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 2                     
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 3                     
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 4                     
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ORQ   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH FAB FRAGMENT                         
DBREF  2A0L A    7   246  UNP    Q9YDF8   KVAP_AERPE      20    259             
DBREF  2A0L B    7   246  UNP    Q9YDF8   KVAP_AERPE      20    259             
DBREF  2A0L C    1   105  PDB    2A0L     2A0L             1    105             
DBREF  2A0L D    1   116  PDB    2A0L     2A0L             1    116             
DBREF  2A0L E    1   105  PDB    2A0L     2A0L             1    105             
DBREF  2A0L F    1   116  PDB    2A0L     2A0L             1    116             
SEQADV 2A0L LEU A    6  UNP  Q9YDF8              CLONING ARTIFACT               
SEQADV 2A0L LEU B    6  UNP  Q9YDF8              CLONING ARTIFACT               
SEQRES   1 A  241  LEU GLY LEU SER ASP LEU GLY GLY ARG VAL ARG ASN ILE          
SEQRES   2 A  241  GLY ASP VAL MET GLU HIS PRO LEU VAL GLU LEU GLY VAL          
SEQRES   3 A  241  SER TYR ALA ALA LEU LEU SER VAL ILE VAL VAL VAL VAL          
SEQRES   4 A  241  GLU TYR THR MET GLN LEU SER GLY GLU TYR LEU VAL ARG          
SEQRES   5 A  241  LEU TYR LEU VAL ASP LEU ILE LEU VAL ILE ILE LEU TRP          
SEQRES   6 A  241  ALA ASP TYR ALA TYR ARG ALA TYR LYS SER GLY ASP PRO          
SEQRES   7 A  241  ALA GLY TYR VAL LYS LYS THR LEU TYR GLU ILE PRO ALA          
SEQRES   8 A  241  LEU VAL PRO ALA GLY LEU LEU ALA LEU ILE GLU GLY HIS          
SEQRES   9 A  241  LEU ALA GLY LEU GLY LEU PHE ARG LEU VAL ARG LEU LEU          
SEQRES  10 A  241  ARG PHE LEU ARG ILE LEU LEU ILE ILE SER ARG GLY SER          
SEQRES  11 A  241  LYS PHE LEU SER ALA ILE ALA ASP ALA ALA ASP LYS ILE          
SEQRES  12 A  241  ARG PHE TYR HIS LEU PHE GLY ALA VAL MET LEU THR VAL          
SEQRES  13 A  241  LEU TYR GLY ALA PHE ALA ILE TYR ILE VAL GLU TYR PRO          
SEQRES  14 A  241  ASP PRO ASN SER SER ILE LYS SER VAL PHE ASP ALA LEU          
SEQRES  15 A  241  TRP TRP ALA VAL VAL THR ALA THR THR VAL GLY TYR GLY          
SEQRES  16 A  241  ASP VAL VAL PRO ALA THR PRO ILE GLY LYS VAL ILE GLY          
SEQRES  17 A  241  ILE ALA VAL MET LEU THR GLY ILE SER ALA LEU THR LEU          
SEQRES  18 A  241  LEU ILE GLY THR VAL SER ASN MET PHE GLN LYS ILE LEU          
SEQRES  19 A  241  VAL GLY GLU PRO GLU PRO SER                                  
SEQRES   1 B  241  LEU GLY LEU SER ASP LEU GLY GLY ARG VAL ARG ASN ILE          
SEQRES   2 B  241  GLY ASP VAL MET GLU HIS PRO LEU VAL GLU LEU GLY VAL          
SEQRES   3 B  241  SER TYR ALA ALA LEU LEU SER VAL ILE VAL VAL VAL VAL          
SEQRES   4 B  241  GLU TYR THR MET GLN LEU SER GLY GLU TYR LEU VAL ARG          
SEQRES   5 B  241  LEU TYR LEU VAL ASP LEU ILE LEU VAL ILE ILE LEU TRP          
SEQRES   6 B  241  ALA ASP TYR ALA TYR ARG ALA TYR LYS SER GLY ASP PRO          
SEQRES   7 B  241  ALA GLY TYR VAL LYS LYS THR LEU TYR GLU ILE PRO ALA          
SEQRES   8 B  241  LEU VAL PRO ALA GLY LEU LEU ALA LEU ILE GLU GLY HIS          
SEQRES   9 B  241  LEU ALA GLY LEU GLY LEU PHE ARG LEU VAL ARG LEU LEU          
SEQRES  10 B  241  ARG PHE LEU ARG ILE LEU LEU ILE ILE SER ARG GLY SER          
SEQRES  11 B  241  LYS PHE LEU SER ALA ILE ALA ASP ALA ALA ASP LYS ILE          
SEQRES  12 B  241  ARG PHE TYR HIS LEU PHE GLY ALA VAL MET LEU THR VAL          
SEQRES  13 B  241  LEU TYR GLY ALA PHE ALA ILE TYR ILE VAL GLU TYR PRO          
SEQRES  14 B  241  ASP PRO ASN SER SER ILE LYS SER VAL PHE ASP ALA LEU          
SEQRES  15 B  241  TRP TRP ALA VAL VAL THR ALA THR THR VAL GLY TYR GLY          
SEQRES  16 B  241  ASP VAL VAL PRO ALA THR PRO ILE GLY LYS VAL ILE GLY          
SEQRES  17 B  241  ILE ALA VAL MET LEU THR GLY ILE SER ALA LEU THR LEU          
SEQRES  18 B  241  LEU ILE GLY THR VAL SER ASN MET PHE GLN LYS ILE LEU          
SEQRES  19 B  241  VAL GLY GLU PRO GLU PRO SER                                  
SEQRES   1 C  105  GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA          
SEQRES   2 C  105  SER LEU GLY ASP ARG VAL THR MET THR CYS THR ALA SER          
SEQRES   3 C  105  SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN          
SEQRES   4 C  105  LYS PRO GLY SER SER PRO LYS LEU TRP ILE TYR SER THR          
SEQRES   5 C  105  SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 C  105  SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER          
SEQRES   7 C  105  MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN          
SEQRES   8 C  105  PHE HIS ARG SER LEU THR PHE GLY SER GLY THR LYS LEU          
SEQRES   9 C  105  GLU                                                          
SEQRES   1 D  116  ASP VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS          
SEQRES   2 D  116  PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY          
SEQRES   3 D  116  TYR SER ILE THR ASN ASN TYR ALA TRP ASN TRP ILE ARG          
SEQRES   4 D  116  GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE          
SEQRES   5 D  116  ASN TYR SER GLY THR THR SER TYR ASN PRO SER LEU LYS          
SEQRES   6 D  116  SER ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN          
SEQRES   7 D  116  PHE PHE LEU GLN LEU ASN SER VAL THR THR GLU ASP THR          
SEQRES   8 D  116  ALA THR TYR PHE CYS VAL ARG GLY TYR ASP TYR PHE ALA          
SEQRES   9 D  116  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL              
SEQRES   1 E  105  GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA          
SEQRES   2 E  105  SER LEU GLY ASP ARG VAL THR MET THR CYS THR ALA SER          
SEQRES   3 E  105  SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN          
SEQRES   4 E  105  LYS PRO GLY SER SER PRO LYS LEU TRP ILE TYR SER THR          
SEQRES   5 E  105  SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 E  105  SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER          
SEQRES   7 E  105  MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN          
SEQRES   8 E  105  PHE HIS ARG SER LEU THR PHE GLY SER GLY THR LYS LEU          
SEQRES   9 E  105  GLU                                                          
SEQRES   1 F  116  ASP VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS          
SEQRES   2 F  116  PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY          
SEQRES   3 F  116  TYR SER ILE THR ASN ASN TYR ALA TRP ASN TRP ILE ARG          
SEQRES   4 F  116  GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE          
SEQRES   5 F  116  ASN TYR SER GLY THR THR SER TYR ASN PRO SER LEU LYS          
SEQRES   6 F  116  SER ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN          
SEQRES   7 F  116  PHE PHE LEU GLN LEU ASN SER VAL THR THR GLU ASP THR          
SEQRES   8 F  116  ALA THR TYR PHE CYS VAL ARG GLY TYR ASP TYR PHE ALA          
SEQRES   9 F  116  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL              
HET      K  B   1       1                                                       
HET      K  A   2       1                                                       
HET      K  A   3       1                                                       
HET      K  B   4       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   7    K    4(K 1+)                                                      
HELIX    1   1 PRO A   25  GLN A   49  1                                  25    
HELIX    2   2 GLU A   53  ILE A   68  1                                  16    
HELIX    3   3 ALA A   84  LYS A   89  1                                   6    
HELIX    4   4 LEU A  103  GLY A  112  1                                  10    
HELIX    5   5 LEU A  115  LEU A  138  1                                  24    
HELIX    6   6 ILE A  148  TYR A  173  1                                  26    
HELIX    7   7 SER A  182  THR A  195  1                                  14    
HELIX    8   8 THR A  206  GLN A  236  1                                  31    
HELIX    9   9 PRO B   25  GLN B   49  1                                  25    
HELIX   10  10 LEU B   55  ILE B   68  1                                  14    
HELIX   11  11 ALA B   84  LYS B   89  1                                   6    
HELIX   12  12 LEU B  103  GLY B  112  1                                  10    
HELIX   13  13 LEU B  115  LEU B  138  1                                  24    
HELIX   14  14 ILE B  148  TYR B  173  1                                  26    
HELIX   15  15 SER B  182  THR B  195  1                                  14    
HELIX   16  16 THR B  206  GLN B  236  1                                  31    
HELIX   17  17 SER D   63  SER D   66  5                                   4    
HELIX   18  18 SER F   63  SER F   66  5                                   4    
SHEET    1   A 4 GLN C   6  SER C   7  0                                        
SHEET    2   A 4 THR C  22  THR C  24 -1  O  THR C  22   N  SER C   7           
SHEET    3   A 4 SER C  71  SER C  73 -1  O  TYR C  72   N  CYS C  23           
SHEET    4   A 4 SER C  66  SER C  68 -1  N  SER C  66   O  SER C  73           
SHEET    1   B 2 ILE C  10  MET C  11  0                                        
SHEET    2   B 2 LYS C 103  LEU C 104  1  O  LYS C 103   N  MET C  11           
SHEET    1   C 5 ASN C  54  LEU C  55  0                                        
SHEET    2   C 5 LYS C  46  TYR C  50 -1  N  TYR C  50   O  ASN C  54           
SHEET    3   C 5 HIS C  35  GLN C  39 -1  N  TRP C  36   O  ILE C  49           
SHEET    4   C 5 THR C  86  PHE C  92 -1  O  TYR C  88   N  TYR C  37           
SHEET    5   C 5 LEU C  96  THR C  97 -1  O  THR C  97   N  GLN C  91           
SHEET    1   D 4 GLN D   3  SER D   7  0                                        
SHEET    2   D 4 LEU D  18  THR D  25 -1  O  THR D  23   N  GLN D   5           
SHEET    3   D 4 GLN D  78  LEU D  83 -1  O  LEU D  83   N  LEU D  18           
SHEET    4   D 4 ILE D  68  ARG D  72 -1  N  THR D  71   O  PHE D  80           
SHEET    1   E 5 THR D  58  TYR D  60  0                                        
SHEET    2   E 5 LEU D  46  ASN D  53 -1  N  TYR D  51   O  SER D  59           
SHEET    3   E 5 ALA D  34  GLN D  40 -1  N  TRP D  35   O  ILE D  52           
SHEET    4   E 5 CYS D  96  TYR D 100 -1  O  GLY D  99   N  ALA D  34           
SHEET    5   E 5 ALA D 104  TRP D 108 -1  O  ASP D 106   N  ARG D  98           
SHEET    1   F 2 ALA D  92  TYR D  94  0                                        
SHEET    2   F 2 THR D 112  VAL D 114 -1  O  VAL D 114   N  ALA D  92           
SHEET    1   G 4 GLN E   6  SER E   7  0                                        
SHEET    2   G 4 THR E  22  THR E  24 -1  O  THR E  22   N  SER E   7           
SHEET    3   G 4 SER E  71  SER E  73 -1  O  TYR E  72   N  CYS E  23           
SHEET    4   G 4 SER E  66  SER E  68 -1  N  SER E  66   O  SER E  73           
SHEET    1   H 2 ILE E  10  MET E  11  0                                        
SHEET    2   H 2 LYS E 103  LEU E 104  1  O  LYS E 103   N  MET E  11           
SHEET    1   I 4 LYS E  46  TYR E  50  0                                        
SHEET    2   I 4 HIS E  35  GLN E  39 -1  N  TRP E  36   O  ILE E  49           
SHEET    3   I 4 THR E  86  PHE E  92 -1  O  TYR E  88   N  TYR E  37           
SHEET    4   I 4 LEU E  96  THR E  97 -1  O  THR E  97   N  GLN E  91           
SHEET    1   J 4 GLN F   3  SER F   7  0                                        
SHEET    2   J 4 LEU F  18  THR F  25 -1  O  THR F  23   N  GLN F   5           
SHEET    3   J 4 GLN F  78  LEU F  83 -1  O  LEU F  83   N  LEU F  18           
SHEET    4   J 4 ILE F  68  ARG F  72 -1  N  THR F  71   O  PHE F  80           
SHEET    1   K 5 THR F  58  TYR F  60  0                                        
SHEET    2   K 5 LEU F  46  ASN F  53 -1  N  TYR F  51   O  SER F  59           
SHEET    3   K 5 ALA F  34  GLN F  40 -1  N  TRP F  35   O  ILE F  52           
SHEET    4   K 5 CYS F  96  TYR F 100 -1  O  GLY F  99   N  ALA F  34           
SHEET    5   K 5 ALA F 104  TRP F 108 -1  O  ASP F 106   N  ARG F  98           
SHEET    1   L 2 ALA F  92  TYR F  94  0                                        
SHEET    2   L 2 THR F 112  VAL F 114 -1  O  VAL F 114   N  ALA F  92           
SSBOND   1 CYS C   23    CYS C   89                          1555   1555  2.03  
SSBOND   2 CYS D   22    CYS D   96                          1555   1555  2.03  
SSBOND   3 CYS E   23    CYS E   89                          1555   1555  2.03  
SSBOND   4 CYS F   22    CYS F   96                          1555   1555  2.04  
LINK         K     K A   2                 O   VAL B 197     1555   1555  3.22  
LINK         K     K A   2                 K     K A   3     1555   1555  3.21  
LINK         K     K A   2                 O   VAL A 197     1555   1555  3.25  
LINK         K     K A   2                 O   GLY B 198     1555   1555  3.05  
LINK         K     K A   2                 K     K B   1     1555   1555  3.40  
LINK         K     K A   2                 O   GLY A 198     1555   1555  3.13  
LINK         K     K A   3                 O   VAL A 197     1555   1555  3.36  
LINK         K     K A   3                 O   THR A 196     1555   1555  3.15  
LINK         K     K A   3                 K     K B   4     1555   1555  3.34  
LINK         K     K A   3                 O   THR B 196     1555   1555  3.10  
LINK         K     K A   3                 O   VAL B 197     1555   1555  3.25  
LINK         K     K B   1                 O   TYR A 199     1555   1555  3.57  
LINK         K     K B   1                 O   TYR B 199     1555   1555  3.50  
LINK         K     K B   4                 OG1 THR A 196     1555   1555  3.54  
LINK         K     K B   4                 O   THR B 196     1555   1555  3.14  
LINK         K     K B   4                 O   THR A 196     1555   1555  3.28  
LINK         K     K B   4                 OG1 THR B 196     1555   1555  3.45  
LINK         K     K A   2                 O   VAL A 197     1555   6565  3.25  
LINK         K     K A   2                 O   VAL B 197     1555   6565  3.22  
LINK         K     K A   2                 K     K A   3     1555   6565  3.21  
LINK         K     K A   2                 O   GLY A 198     1555   6565  3.13  
LINK         K     K A   2                 O   GLY B 198     1555   6565  3.05  
LINK         K     K A   2                 K     K B   1     1555   6565  3.40  
LINK         K     K A   3                 K     K B   4     1555   6565  3.34  
LINK         K     K A   3                 O   THR A 196     1555   6565  3.15  
LINK         K     K A   3                 O   VAL A 197     1555   6565  3.36  
LINK         K     K A   3                 O   THR B 196     1555   6565  3.10  
LINK         K     K A   3                 O   VAL B 197     1555   6565  3.25  
LINK         K     K B   1                 O   TYR B 199     1555   6565  3.50  
LINK         K     K B   1                 O   TYR A 199     1555   6565  3.57  
LINK         K     K B   4                 OG1 THR A 196     1555   6565  3.54  
LINK         K     K B   4                 OG1 THR B 196     1555   6565  3.45  
LINK         K     K B   4                 O   THR A 196     1555   6565  3.28  
LINK         K     K B   4                 O   THR B 196     1555   6565  3.14  
CISPEP   1 SER C    7    PRO C    8          0        -0.12                     
CISPEP   2 SER E    7    PRO E    8          0        -0.18                     
SITE     1 AC1  3   K A   2  TYR A 199  TYR B 199                               
SITE     1 AC2  6   K A   3  VAL A 197  GLY A 198    K B   1                    
SITE     2 AC2  6 VAL B 197  GLY B 198                                          
SITE     1 AC3  6   K A   2  THR A 196  VAL A 197    K B   4                    
SITE     2 AC3  6 THR B 196  VAL B 197                                          
SITE     1 AC4  3   K A   3  THR A 196  THR B 196                               
CRYST1  136.362  136.362  191.812  90.00  90.00  90.00 P 42 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      0.007333  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007333  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005213        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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