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Database: PDB
Entry: 5BUT
LinkDB: 5BUT
Original site: 5BUT 
HEADER    MEMBRANE PROTEIN                        04-JUN-15   5BUT              
TITLE     CRYSTAL STRUCTURE OF INACTIVE CONFORMATION OF KTRAB K+ TRANSPORTER    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KTR SYSTEM POTASSIUM UPTAKE PROTEIN A,KTR SYSTEM POTASSIUM 
COMPND   3 UPTAKE PROTEIN A;                                                    
COMPND   4 CHAIN: A, C, E, G;                                                   
COMPND   5 FRAGMENT: REGULATORY DOMAIN,REGULATORY DOMAIN;                       
COMPND   6 SYNONYM: K(+)-UPTAKE PROTEIN KTRA,K(+)-UPTAKE PROTEIN KTRA;          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: KTRA DELTA C IS A FUSION OF TWO N-TERMINAL DOMAINS OF 
COMPND  10 KTRA THROUGH THE LINKER LEGS. IT ALSO INCLUDES A C TO V MUTATION.;   
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: KTR SYSTEM POTASSIUM UPTAKE PROTEIN B;                     
COMPND  13 CHAIN: I, J, K, L;                                                   
COMPND  14 FRAGMENT: MEMBRANE PROTEIN;                                          
COMPND  15 SYNONYM: K(+)-UPTAKE PROTEIN KTRB;                                   
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: KTRA, YUAA, BSU31090;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET24;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  11 ORGANISM_TAXID: 1423;                                                
SOURCE  12 GENE: KTRB, YUBG, BSU31100;                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET24                                     
KEYWDS    MEMBRANE PROTEIN COMPLEX, MEMBRANE PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.S.VIEIRA-PIRES,J.H.MORAIS-CABRAL                                    
REVDAT   1   27-JAN-16 5BUT    0                                                
JRNL        AUTH   A.SZOLLOSI,R.S.VIEIRA-PIRES,C.M.TEIXEIRA-DUARTE,R.ROCHA,     
JRNL        AUTH 2 J.H.MORAIS-CABRAL                                            
JRNL        TITL   DISSECTING THE MOLECULAR MECHANISM OF NUCLEOTIDE-DEPENDENT   
JRNL        TITL 2 ACTIVATION OF THE KTRAB K+ TRANSPORTER.                      
JRNL        REF    PLOS BIOL.                    V.  14 02356 2016              
JRNL        REFN                   ESSN 1545-7885                               
JRNL        PMID   26771197                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1002356                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS DENR                                             
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 200.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 12628                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM SELECTION                
REMARK   3   R VALUE            (WORKING SET) : 0.325                           
REMARK   3   FREE R VALUE                     : 0.339                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2316                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 5.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 6.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1978                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4540                       
REMARK   3   BIN FREE R VALUE                    : 0.5028                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 260                          
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            : 21472                                   
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) : 343.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -142.74200                                           
REMARK   3    B22 (A**2) : 58.29400                                             
REMARK   3    B33 (A**2) : 84.44800                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -25.03200                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.003                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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        : 261.7                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:CARBOHYDRATE.PARAM                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5BUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210540.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12628                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 200.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.82200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: KTRB FROM 4J7C AND KTRA-DELTAC FROM 2HMS             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 16-22% PEG 400, 100     
REMARK 280  -200 MM CACL2, PH 8.5, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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  1.000000  0.000000  0.000000      153.53000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      153.53000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G, I, J                      
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     VAL A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     ASN A   143                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     LEU A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     LEU A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     LEU A   285                                                      
REMARK 465     VAL A   286                                                      
REMARK 465     PRO A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     VAL C   141                                                      
REMARK 465     LEU C   142                                                      
REMARK 465     ASN C   143                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     LEU C   145                                                      
REMARK 465     GLU C   146                                                      
REMARK 465     GLY C   147                                                      
REMARK 465     SER C   148                                                      
REMARK 465     LEU C   283                                                      
REMARK 465     GLU C   284                                                      
REMARK 465     LEU C   285                                                      
REMARK 465     VAL C   286                                                      
REMARK 465     PRO C   287                                                      
REMARK 465     ARG C   288                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     ILE E     4                                                      
REMARK 465     LYS E     5                                                      
REMARK 465     ASN E     6                                                      
REMARK 465     VAL E   141                                                      
REMARK 465     LEU E   142                                                      
REMARK 465     ASN E   143                                                      
REMARK 465     TYR E   144                                                      
REMARK 465     LEU E   145                                                      
REMARK 465     GLU E   146                                                      
REMARK 465     GLY E   147                                                      
REMARK 465     SER E   148                                                      
REMARK 465     LEU E   283                                                      
REMARK 465     GLU E   284                                                      
REMARK 465     LEU E   285                                                      
REMARK 465     VAL E   286                                                      
REMARK 465     PRO E   287                                                      
REMARK 465     ARG E   288                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     ILE G     4                                                      
REMARK 465     LYS G     5                                                      
REMARK 465     ASN G     6                                                      
REMARK 465     VAL G   141                                                      
REMARK 465     LEU G   142                                                      
REMARK 465     ASN G   143                                                      
REMARK 465     TYR G   144                                                      
REMARK 465     LEU G   145                                                      
REMARK 465     GLU G   146                                                      
REMARK 465     GLY G   147                                                      
REMARK 465     SER G   148                                                      
REMARK 465     LEU G   283                                                      
REMARK 465     GLU G   284                                                      
REMARK 465     LEU G   285                                                      
REMARK 465     VAL G   286                                                      
REMARK 465     PRO G   287                                                      
REMARK 465     ARG G   288                                                      
REMARK 465     MET I     1                                                      
REMARK 465     THR I     2                                                      
REMARK 465     LEU I     3                                                      
REMARK 465     GLN I     4                                                      
REMARK 465     LYS I     5                                                      
REMARK 465     ASP I     6                                                      
REMARK 465     LYS I     7                                                      
REMARK 465     VAL I     8                                                      
REMARK 465     ILE I     9                                                      
REMARK 465     LYS I    10                                                      
REMARK 465     TRP I    11                                                      
REMARK 465     VAL I    12                                                      
REMARK 465     ARG I    13                                                      
REMARK 465     PHE I    14                                                      
REMARK 465     MET J     1                                                      
REMARK 465     THR J     2                                                      
REMARK 465     LEU J     3                                                      
REMARK 465     GLN J     4                                                      
REMARK 465     LYS J     5                                                      
REMARK 465     ASP J     6                                                      
REMARK 465     LYS J     7                                                      
REMARK 465     VAL J     8                                                      
REMARK 465     ILE J     9                                                      
REMARK 465     LYS J    10                                                      
REMARK 465     TRP J    11                                                      
REMARK 465     VAL J    12                                                      
REMARK 465     ARG J    13                                                      
REMARK 465     PHE J    14                                                      
REMARK 465     MET K     1                                                      
REMARK 465     THR K     2                                                      
REMARK 465     LEU K     3                                                      
REMARK 465     GLN K     4                                                      
REMARK 465     LYS K     5                                                      
REMARK 465     ASP K     6                                                      
REMARK 465     LYS K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ILE K     9                                                      
REMARK 465     LYS K    10                                                      
REMARK 465     TRP K    11                                                      
REMARK 465     VAL K    12                                                      
REMARK 465     ARG K    13                                                      
REMARK 465     PHE K    14                                                      
REMARK 465     MET L     1                                                      
REMARK 465     THR L     2                                                      
REMARK 465     LEU L     3                                                      
REMARK 465     GLN L     4                                                      
REMARK 465     LYS L     5                                                      
REMARK 465     ASP L     6                                                      
REMARK 465     LYS L     7                                                      
REMARK 465     VAL L     8                                                      
REMARK 465     ILE L     9                                                      
REMARK 465     LYS L    10                                                      
REMARK 465     TRP L    11                                                      
REMARK 465     VAL L    12                                                      
REMARK 465     ARG L    13                                                      
REMARK 465     PHE L    14                                                      
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    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG C 120   CD  -  NE  -  CZ  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG C 120   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG C 120   NE  -  CZ  -  NH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG E 120   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG E 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG E 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG G 120   CD  -  NE  -  CZ  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG G 120   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG G 120   NE  -  CZ  -  NH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG G 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG G 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    LEU A  14       43.41    -92.05                                   
REMARK 500    ALA A  80     -123.54     26.72                                   
REMARK 500    ASN A  81       91.01    -30.93                                   
REMARK 500    THR A  86      -71.01    -66.00                                   
REMARK 500    GLN A 105      -69.49    -96.48                                   
REMARK 500    ARG A 120      140.71   -170.42                                   
REMARK 500    LEU A 156       41.09    -91.45                                   
REMARK 500    ALA A 222     -125.68     25.07                                   
REMARK 500    ASN A 223       90.84    -28.68                                   
REMARK 500    THR A 228      -70.12    -69.42                                   
REMARK 500    GLN A 247      -70.36    -95.48                                   
REMARK 500    ARG A 262      136.62   -170.75                                   
REMARK 500    LEU C  14       41.08    -92.41                                   
REMARK 500    ALA C  80     -123.99     25.70                                   
REMARK 500    ASN C  81       91.09    -31.56                                   
REMARK 500    THR C  86      -72.23    -64.19                                   
REMARK 500    GLN C 105      -69.29    -95.36                                   
REMARK 500    ARG C 120      137.75   -173.14                                   
REMARK 500    LEU C 156       42.06    -91.15                                   
REMARK 500    VAL C 177      128.54   -171.17                                   
REMARK 500    ALA C 222     -126.02     25.83                                   
REMARK 500    ASN C 223       90.27    -27.76                                   
REMARK 500    THR C 228      -70.45    -64.98                                   
REMARK 500    GLN C 247      -70.81    -96.89                                   
REMARK 500    ARG C 262      138.19   -170.83                                   
REMARK 500    LEU E  14       43.09    -90.19                                   
REMARK 500    ALA E  80     -125.26     25.52                                   
REMARK 500    ASN E  81       90.26    -29.57                                   
REMARK 500    THR E  86      -70.41    -69.84                                   
REMARK 500    GLN E 105      -70.20    -94.24                                   
REMARK 500    ARG E 120      138.23   -170.30                                   
REMARK 500    LEU E 156       42.02    -92.89                                   
REMARK 500    ALA E 222     -126.99     26.74                                   
REMARK 500    ASN E 223       89.72    -28.35                                   
REMARK 500    THR E 228      -74.03    -64.05                                   
REMARK 500    GLN E 247      -67.18    -98.13                                   
REMARK 500    ARG E 262      139.35   -171.57                                   
REMARK 500    LEU G  14       41.55    -92.44                                   
REMARK 500    ALA G  80     -125.44     25.34                                   
REMARK 500    ASN G  81       91.58    -29.64                                   
REMARK 500    GLN G 105      -71.46    -95.36                                   
REMARK 500    ARG G 120      138.67   -170.85                                   
REMARK 500    LEU G 156       41.89    -93.29                                   
REMARK 500    ALA G 222     -125.71     27.88                                   
REMARK 500    ASN G 223       90.96    -29.73                                   
REMARK 500    THR G 228      -72.07    -64.18                                   
REMARK 500    GLN G 247      -68.29    -97.98                                   
REMARK 500    ARG G 262      138.50   -171.09                                   
REMARK 500    THR I  42      -71.22    -77.11                                   
REMARK 500    ASP I  49       22.32    -78.26                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     249 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K I 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR I  61   O                                                      
REMARK 620 2 ASN I 175   O   128.7                                              
REMARK 620 3 ALA I 176   O    75.8  82.7                                        
REMARK 620 4 THR I 278   O   146.8  63.1 136.4                                  
REMARK 620 5 ALA I 279   O   133.3  85.3  79.0  72.4                            
REMARK 620 6 THR I 390   O    73.5  95.3 138.4  74.6 142.5                      
REMARK 620 7 VAL I 391   O    78.7 150.2 119.8  87.5  80.9  80.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K J 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL J  60   O                                                      
REMARK 620 2 THR J  61   O    87.1                                              
REMARK 620 3 ASN J 175   O    60.6 143.2                                        
REMARK 620 4 ALA J 176   O    86.6  74.2  86.0                                  
REMARK 620 5 THR J 278   O   110.1 148.5  66.1 131.0                            
REMARK 620 6 THR J 390   O    79.5  79.8 108.4 151.1  77.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K K 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN K 175   O                                                      
REMARK 620 2 THR K 278   O    75.9                                              
REMARK 620 3 ALA K 279   O    91.2  81.3                                        
REMARK 620 4 THR K 390   O   103.7  92.9 162.2                                  
REMARK 620 5 VAL K 391   O   173.1 102.0  81.9  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K L 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL L  60   O                                                      
REMARK 620 2 THR L  61   O    90.1                                              
REMARK 620 3 ASN L 175   O    66.5 150.3                                        
REMARK 620 4 ALA L 176   O    92.0  72.6  89.4                                  
REMARK 620 5 THR L 278   O   116.0 141.3  68.2 129.9                            
REMARK 620 6 THR L 390   O    82.8  78.7 114.2 150.7  77.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K I 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K J 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K K 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 501                   
DBREF  5BUT A    1   144  UNP    O32080   KTRA_BACSU       1    144             
DBREF  5BUT A  149   282  UNP    O32080   KTRA_BACSU       7    140             
DBREF  5BUT C    1   144  UNP    O32080   KTRA_BACSU       1    144             
DBREF  5BUT C  149   282  UNP    O32080   KTRA_BACSU       7    140             
DBREF  5BUT E    1   144  UNP    O32080   KTRA_BACSU       1    144             
DBREF  5BUT E  149   282  UNP    O32080   KTRA_BACSU       7    140             
DBREF  5BUT G    1   144  UNP    O32080   KTRA_BACSU       1    144             
DBREF  5BUT G  149   282  UNP    O32080   KTRA_BACSU       7    140             
DBREF  5BUT I    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  5BUT J    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  5BUT K    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  5BUT L    1   445  UNP    O32081   KTRB_BACSU       1    445             
SEQADV 5BUT LEU A  145  UNP  O32080              LINKER                         
SEQADV 5BUT GLU A  146  UNP  O32080              LINKER                         
SEQADV 5BUT GLY A  147  UNP  O32080              LINKER                         
SEQADV 5BUT SER A  148  UNP  O32080              LINKER                         
SEQADV 5BUT LEU A  283  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT GLU A  284  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT LEU A  285  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL A  286  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT PRO A  287  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT ARG A  288  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL A   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 5BUT LEU C  145  UNP  O32080              LINKER                         
SEQADV 5BUT GLU C  146  UNP  O32080              LINKER                         
SEQADV 5BUT GLY C  147  UNP  O32080              LINKER                         
SEQADV 5BUT SER C  148  UNP  O32080              LINKER                         
SEQADV 5BUT LEU C  283  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT GLU C  284  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT LEU C  285  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL C  286  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT PRO C  287  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT ARG C  288  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL C   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 5BUT LEU E  145  UNP  O32080              LINKER                         
SEQADV 5BUT GLU E  146  UNP  O32080              LINKER                         
SEQADV 5BUT GLY E  147  UNP  O32080              LINKER                         
SEQADV 5BUT SER E  148  UNP  O32080              LINKER                         
SEQADV 5BUT LEU E  283  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT GLU E  284  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT LEU E  285  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL E  286  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT PRO E  287  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT ARG E  288  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL E   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 5BUT LEU G  145  UNP  O32080              LINKER                         
SEQADV 5BUT GLU G  146  UNP  O32080              LINKER                         
SEQADV 5BUT GLY G  147  UNP  O32080              LINKER                         
SEQADV 5BUT SER G  148  UNP  O32080              LINKER                         
SEQADV 5BUT LEU G  283  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT GLU G  284  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT LEU G  285  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL G  286  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT PRO G  287  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT ARG G  288  UNP  O32080              EXPRESSION TAG                 
SEQADV 5BUT VAL G   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 5BUT ALA I  103  UNP  O32081    GLY   103 CONFLICT                       
SEQADV 5BUT ALA I  104  UNP  O32081    LYS   104 CONFLICT                       
SEQADV 5BUT ALA I  105  UNP  O32081    LYS   105 CONFLICT                       
SEQADV 5BUT GLN I  218  UNP  O32081    ASN   218 CONFLICT                       
SEQADV 5BUT ALA I  229  UNP  O32081    LYS   229 CONFLICT                       
SEQADV 5BUT ALA I  261  UNP  O32081    HIS   261 CONFLICT                       
SEQADV 5BUT ALA I  262  UNP  O32081    ILE   262 CONFLICT                       
SEQADV 5BUT ALA I  429  UNP  O32081    LYS   429 CONFLICT                       
SEQADV 5BUT ALA J  103  UNP  O32081    GLY   103 CONFLICT                       
SEQADV 5BUT ALA J  104  UNP  O32081    LYS   104 CONFLICT                       
SEQADV 5BUT ALA J  105  UNP  O32081    LYS   105 CONFLICT                       
SEQADV 5BUT GLN J  218  UNP  O32081    ASN   218 CONFLICT                       
SEQADV 5BUT ALA J  229  UNP  O32081    LYS   229 CONFLICT                       
SEQADV 5BUT ALA J  261  UNP  O32081    HIS   261 CONFLICT                       
SEQADV 5BUT ALA J  262  UNP  O32081    ILE   262 CONFLICT                       
SEQADV 5BUT ALA J  429  UNP  O32081    LYS   429 CONFLICT                       
SEQADV 5BUT ALA K  103  UNP  O32081    GLY   103 CONFLICT                       
SEQADV 5BUT ALA K  104  UNP  O32081    LYS   104 CONFLICT                       
SEQADV 5BUT ALA K  105  UNP  O32081    LYS   105 CONFLICT                       
SEQADV 5BUT GLN K  218  UNP  O32081    ASN   218 CONFLICT                       
SEQADV 5BUT ALA K  229  UNP  O32081    LYS   229 CONFLICT                       
SEQADV 5BUT ALA K  261  UNP  O32081    HIS   261 CONFLICT                       
SEQADV 5BUT ALA K  262  UNP  O32081    ILE   262 CONFLICT                       
SEQADV 5BUT ALA K  429  UNP  O32081    LYS   429 CONFLICT                       
SEQADV 5BUT ALA L  103  UNP  O32081    GLY   103 CONFLICT                       
SEQADV 5BUT ALA L  104  UNP  O32081    LYS   104 CONFLICT                       
SEQADV 5BUT ALA L  105  UNP  O32081    LYS   105 CONFLICT                       
SEQADV 5BUT GLN L  218  UNP  O32081    ASN   218 CONFLICT                       
SEQADV 5BUT ALA L  229  UNP  O32081    LYS   229 CONFLICT                       
SEQADV 5BUT ALA L  261  UNP  O32081    HIS   261 CONFLICT                       
SEQADV 5BUT ALA L  262  UNP  O32081    ILE   262 CONFLICT                       
SEQADV 5BUT ALA L  429  UNP  O32081    LYS   429 CONFLICT                       
SEQRES   1 A  288  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 A  288  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 A  288  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 A  288  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 A  288  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 A  288  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 A  288  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 A  288  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 A  288  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 A  288  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 A  288  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 A  288  TYR LEU GLU GLY SER LYS GLN PHE ALA VAL ILE GLY LEU          
SEQRES  13 A  288  GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS ARG          
SEQRES  14 A  288  MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU GLU          
SEQRES  15 A  288  LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA VAL          
SEQRES  16 A  288  ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER LEU          
SEQRES  17 A  288  GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE GLY          
SEQRES  18 A  288  ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU LEU          
SEQRES  19 A  288  LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA GLN          
SEQRES  20 A  288  ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY ALA          
SEQRES  21 A  288  ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL LYS          
SEQRES  22 A  288  ILE ALA GLN SER LEU SER ASP GLU ASN LEU GLU LEU VAL          
SEQRES  23 A  288  PRO ARG                                                      
SEQRES   1 C  288  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 C  288  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 C  288  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 C  288  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 C  288  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 C  288  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 C  288  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 C  288  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 C  288  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 C  288  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 C  288  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 C  288  TYR LEU GLU GLY SER LYS GLN PHE ALA VAL ILE GLY LEU          
SEQRES  13 C  288  GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS ARG          
SEQRES  14 C  288  MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU GLU          
SEQRES  15 C  288  LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA VAL          
SEQRES  16 C  288  ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER LEU          
SEQRES  17 C  288  GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE GLY          
SEQRES  18 C  288  ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU LEU          
SEQRES  19 C  288  LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA GLN          
SEQRES  20 C  288  ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY ALA          
SEQRES  21 C  288  ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL LYS          
SEQRES  22 C  288  ILE ALA GLN SER LEU SER ASP GLU ASN LEU GLU LEU VAL          
SEQRES  23 C  288  PRO ARG                                                      
SEQRES   1 E  288  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 E  288  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 E  288  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 E  288  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 E  288  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 E  288  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 E  288  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 E  288  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 E  288  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 E  288  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 E  288  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 E  288  TYR LEU GLU GLY SER LYS GLN PHE ALA VAL ILE GLY LEU          
SEQRES  13 E  288  GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS ARG          
SEQRES  14 E  288  MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU GLU          
SEQRES  15 E  288  LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA VAL          
SEQRES  16 E  288  ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER LEU          
SEQRES  17 E  288  GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE GLY          
SEQRES  18 E  288  ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU LEU          
SEQRES  19 E  288  LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA GLN          
SEQRES  20 E  288  ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY ALA          
SEQRES  21 E  288  ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL LYS          
SEQRES  22 E  288  ILE ALA GLN SER LEU SER ASP GLU ASN LEU GLU LEU VAL          
SEQRES  23 E  288  PRO ARG                                                      
SEQRES   1 G  288  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 G  288  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 G  288  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 G  288  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 G  288  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 G  288  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 G  288  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 G  288  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 G  288  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 G  288  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 G  288  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 G  288  TYR LEU GLU GLY SER LYS GLN PHE ALA VAL ILE GLY LEU          
SEQRES  13 G  288  GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS ARG          
SEQRES  14 G  288  MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU GLU          
SEQRES  15 G  288  LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA VAL          
SEQRES  16 G  288  ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER LEU          
SEQRES  17 G  288  GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE GLY          
SEQRES  18 G  288  ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU LEU          
SEQRES  19 G  288  LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA GLN          
SEQRES  20 G  288  ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY ALA          
SEQRES  21 G  288  ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL LYS          
SEQRES  22 G  288  ILE ALA GLN SER LEU SER ASP GLU ASN LEU GLU LEU VAL          
SEQRES  23 G  288  PRO ARG                                                      
SEQRES   1 I  445  MET THR LEU GLN LYS ASP LYS VAL ILE LYS TRP VAL ARG          
SEQRES   2 I  445  PHE THR PRO PRO GLN VAL LEU ALA ILE GLY PHE PHE LEU          
SEQRES   3 I  445  THR ILE ILE ILE GLY ALA VAL LEU LEU MET LEU PRO ILE          
SEQRES   4 I  445  SER THR THR LYS PRO LEU SER TRP ILE ASP ALA LEU PHE          
SEQRES   5 I  445  THR ALA ALA SER ALA THR THR VAL THR GLY LEU ALA VAL          
SEQRES   6 I  445  VAL ASP THR GLY THR GLN PHE THR VAL PHE GLY GLN THR          
SEQRES   7 I  445  VAL ILE MET GLY LEU ILE GLN ILE GLY GLY LEU GLY PHE          
SEQRES   8 I  445  MET THR PHE ALA VAL LEU ILE VAL MET ILE LEU ALA ALA          
SEQRES   9 I  445  ALA ILE GLY LEU LYS GLU ARG MET LEU VAL GLN GLU ALA          
SEQRES  10 I  445  LEU ASN GLN PRO THR ILE GLY GLY VAL ILE GLY LEU VAL          
SEQRES  11 I  445  LYS VAL LEU PHE LEU PHE SER ILE SER ILE GLU LEU ILE          
SEQRES  12 I  445  ALA ALA LEU ILE LEU SER ILE ARG LEU VAL PRO GLN TYR          
SEQRES  13 I  445  GLY TRP SER SER GLY LEU PHE ALA SER LEU PHE HIS ALA          
SEQRES  14 I  445  ILE SER ALA PHE ASN ASN ALA GLY PHE SER LEU TRP PRO          
SEQRES  15 I  445  ASP ASN LEU MET SER TYR VAL GLY ASP PRO THR VAL ASN          
SEQRES  16 I  445  LEU VAL ILE THR PHE LEU PHE ILE THR GLY GLY ILE GLY          
SEQRES  17 I  445  PHE THR VAL LEU PHE ASP VAL MET LYS GLN ARG ARG PHE          
SEQRES  18 I  445  LYS THR PHE SER LEU HIS THR ALA LEU MET LEU THR GLY          
SEQRES  19 I  445  THR LEU MET LEU ASN ALA ILE ALA MET LEU THR VAL PHE          
SEQRES  20 I  445  ILE LEU GLU TYR SER ASN PRO GLY THR LEU GLY HIS LEU          
SEQRES  21 I  445  ALA ALA VAL ASP LYS LEU TRP ALA SER TYR PHE GLN ALA          
SEQRES  22 I  445  VAL THR PRO ARG THR ALA GLY PHE ASN SER LEU ASP PHE          
SEQRES  23 I  445  GLY SER MET ARG GLU GLY THR ILE VAL PHE THR LEU LEU          
SEQRES  24 I  445  LEU MET PHE ILE GLY ALA GLY SER ALA SER THR ALA SER          
SEQRES  25 I  445  GLY ILE LYS LEU THR THR PHE ILE VAL ILE LEU THR SER          
SEQRES  26 I  445  VAL ILE ALA TYR LEU ARG GLY LYS LYS GLU THR VAL ILE          
SEQRES  27 I  445  PHE ARG ARG SER ILE LYS TYR PRO ILE ILE ILE LYS ALA          
SEQRES  28 I  445  LEU ALA VAL SER VAL THR SER LEU PHE ILE VAL PHE LEU          
SEQRES  29 I  445  GLY ILE PHE ALA LEU THR ILE THR GLU GLN ALA PRO PHE          
SEQRES  30 I  445  LEU GLN ILE VAL PHE GLU THR PHE SER ALA PHE GLY THR          
SEQRES  31 I  445  VAL GLY LEU THR MET GLY LEU THR PRO GLU LEU THR THR          
SEQRES  32 I  445  ALA GLY LYS CYS ILE ILE ILE VAL ILE MET PHE ILE GLY          
SEQRES  33 I  445  ARG ILE GLY PRO LEU THR PHE VAL PHE SER PHE ALA ALA          
SEQRES  34 I  445  THR GLU GLN SER ASN ILE ARG TYR PRO ASP GLY GLU VAL          
SEQRES  35 I  445  PHE THR GLY                                                  
SEQRES   1 J  445  MET THR LEU GLN LYS ASP LYS VAL ILE LYS TRP VAL ARG          
SEQRES   2 J  445  PHE THR PRO PRO GLN VAL LEU ALA ILE GLY PHE PHE LEU          
SEQRES   3 J  445  THR ILE ILE ILE GLY ALA VAL LEU LEU MET LEU PRO ILE          
SEQRES   4 J  445  SER THR THR LYS PRO LEU SER TRP ILE ASP ALA LEU PHE          
SEQRES   5 J  445  THR ALA ALA SER ALA THR THR VAL THR GLY LEU ALA VAL          
SEQRES   6 J  445  VAL ASP THR GLY THR GLN PHE THR VAL PHE GLY GLN THR          
SEQRES   7 J  445  VAL ILE MET GLY LEU ILE GLN ILE GLY GLY LEU GLY PHE          
SEQRES   8 J  445  MET THR PHE ALA VAL LEU ILE VAL MET ILE LEU ALA ALA          
SEQRES   9 J  445  ALA ILE GLY LEU LYS GLU ARG MET LEU VAL GLN GLU ALA          
SEQRES  10 J  445  LEU ASN GLN PRO THR ILE GLY GLY VAL ILE GLY LEU VAL          
SEQRES  11 J  445  LYS VAL LEU PHE LEU PHE SER ILE SER ILE GLU LEU ILE          
SEQRES  12 J  445  ALA ALA LEU ILE LEU SER ILE ARG LEU VAL PRO GLN TYR          
SEQRES  13 J  445  GLY TRP SER SER GLY LEU PHE ALA SER LEU PHE HIS ALA          
SEQRES  14 J  445  ILE SER ALA PHE ASN ASN ALA GLY PHE SER LEU TRP PRO          
SEQRES  15 J  445  ASP ASN LEU MET SER TYR VAL GLY ASP PRO THR VAL ASN          
SEQRES  16 J  445  LEU VAL ILE THR PHE LEU PHE ILE THR GLY GLY ILE GLY          
SEQRES  17 J  445  PHE THR VAL LEU PHE ASP VAL MET LYS GLN ARG ARG PHE          
SEQRES  18 J  445  LYS THR PHE SER LEU HIS THR ALA LEU MET LEU THR GLY          
SEQRES  19 J  445  THR LEU MET LEU ASN ALA ILE ALA MET LEU THR VAL PHE          
SEQRES  20 J  445  ILE LEU GLU TYR SER ASN PRO GLY THR LEU GLY HIS LEU          
SEQRES  21 J  445  ALA ALA VAL ASP LYS LEU TRP ALA SER TYR PHE GLN ALA          
SEQRES  22 J  445  VAL THR PRO ARG THR ALA GLY PHE ASN SER LEU ASP PHE          
SEQRES  23 J  445  GLY SER MET ARG GLU GLY THR ILE VAL PHE THR LEU LEU          
SEQRES  24 J  445  LEU MET PHE ILE GLY ALA GLY SER ALA SER THR ALA SER          
SEQRES  25 J  445  GLY ILE LYS LEU THR THR PHE ILE VAL ILE LEU THR SER          
SEQRES  26 J  445  VAL ILE ALA TYR LEU ARG GLY LYS LYS GLU THR VAL ILE          
SEQRES  27 J  445  PHE ARG ARG SER ILE LYS TYR PRO ILE ILE ILE LYS ALA          
SEQRES  28 J  445  LEU ALA VAL SER VAL THR SER LEU PHE ILE VAL PHE LEU          
SEQRES  29 J  445  GLY ILE PHE ALA LEU THR ILE THR GLU GLN ALA PRO PHE          
SEQRES  30 J  445  LEU GLN ILE VAL PHE GLU THR PHE SER ALA PHE GLY THR          
SEQRES  31 J  445  VAL GLY LEU THR MET GLY LEU THR PRO GLU LEU THR THR          
SEQRES  32 J  445  ALA GLY LYS CYS ILE ILE ILE VAL ILE MET PHE ILE GLY          
SEQRES  33 J  445  ARG ILE GLY PRO LEU THR PHE VAL PHE SER PHE ALA ALA          
SEQRES  34 J  445  THR GLU GLN SER ASN ILE ARG TYR PRO ASP GLY GLU VAL          
SEQRES  35 J  445  PHE THR GLY                                                  
SEQRES   1 K  445  MET THR LEU GLN LYS ASP LYS VAL ILE LYS TRP VAL ARG          
SEQRES   2 K  445  PHE THR PRO PRO GLN VAL LEU ALA ILE GLY PHE PHE LEU          
SEQRES   3 K  445  THR ILE ILE ILE GLY ALA VAL LEU LEU MET LEU PRO ILE          
SEQRES   4 K  445  SER THR THR LYS PRO LEU SER TRP ILE ASP ALA LEU PHE          
SEQRES   5 K  445  THR ALA ALA SER ALA THR THR VAL THR GLY LEU ALA VAL          
SEQRES   6 K  445  VAL ASP THR GLY THR GLN PHE THR VAL PHE GLY GLN THR          
SEQRES   7 K  445  VAL ILE MET GLY LEU ILE GLN ILE GLY GLY LEU GLY PHE          
SEQRES   8 K  445  MET THR PHE ALA VAL LEU ILE VAL MET ILE LEU ALA ALA          
SEQRES   9 K  445  ALA ILE GLY LEU LYS GLU ARG MET LEU VAL GLN GLU ALA          
SEQRES  10 K  445  LEU ASN GLN PRO THR ILE GLY GLY VAL ILE GLY LEU VAL          
SEQRES  11 K  445  LYS VAL LEU PHE LEU PHE SER ILE SER ILE GLU LEU ILE          
SEQRES  12 K  445  ALA ALA LEU ILE LEU SER ILE ARG LEU VAL PRO GLN TYR          
SEQRES  13 K  445  GLY TRP SER SER GLY LEU PHE ALA SER LEU PHE HIS ALA          
SEQRES  14 K  445  ILE SER ALA PHE ASN ASN ALA GLY PHE SER LEU TRP PRO          
SEQRES  15 K  445  ASP ASN LEU MET SER TYR VAL GLY ASP PRO THR VAL ASN          
SEQRES  16 K  445  LEU VAL ILE THR PHE LEU PHE ILE THR GLY GLY ILE GLY          
SEQRES  17 K  445  PHE THR VAL LEU PHE ASP VAL MET LYS GLN ARG ARG PHE          
SEQRES  18 K  445  LYS THR PHE SER LEU HIS THR ALA LEU MET LEU THR GLY          
SEQRES  19 K  445  THR LEU MET LEU ASN ALA ILE ALA MET LEU THR VAL PHE          
SEQRES  20 K  445  ILE LEU GLU TYR SER ASN PRO GLY THR LEU GLY HIS LEU          
SEQRES  21 K  445  ALA ALA VAL ASP LYS LEU TRP ALA SER TYR PHE GLN ALA          
SEQRES  22 K  445  VAL THR PRO ARG THR ALA GLY PHE ASN SER LEU ASP PHE          
SEQRES  23 K  445  GLY SER MET ARG GLU GLY THR ILE VAL PHE THR LEU LEU          
SEQRES  24 K  445  LEU MET PHE ILE GLY ALA GLY SER ALA SER THR ALA SER          
SEQRES  25 K  445  GLY ILE LYS LEU THR THR PHE ILE VAL ILE LEU THR SER          
SEQRES  26 K  445  VAL ILE ALA TYR LEU ARG GLY LYS LYS GLU THR VAL ILE          
SEQRES  27 K  445  PHE ARG ARG SER ILE LYS TYR PRO ILE ILE ILE LYS ALA          
SEQRES  28 K  445  LEU ALA VAL SER VAL THR SER LEU PHE ILE VAL PHE LEU          
SEQRES  29 K  445  GLY ILE PHE ALA LEU THR ILE THR GLU GLN ALA PRO PHE          
SEQRES  30 K  445  LEU GLN ILE VAL PHE GLU THR PHE SER ALA PHE GLY THR          
SEQRES  31 K  445  VAL GLY LEU THR MET GLY LEU THR PRO GLU LEU THR THR          
SEQRES  32 K  445  ALA GLY LYS CYS ILE ILE ILE VAL ILE MET PHE ILE GLY          
SEQRES  33 K  445  ARG ILE GLY PRO LEU THR PHE VAL PHE SER PHE ALA ALA          
SEQRES  34 K  445  THR GLU GLN SER ASN ILE ARG TYR PRO ASP GLY GLU VAL          
SEQRES  35 K  445  PHE THR GLY                                                  
SEQRES   1 L  445  MET THR LEU GLN LYS ASP LYS VAL ILE LYS TRP VAL ARG          
SEQRES   2 L  445  PHE THR PRO PRO GLN VAL LEU ALA ILE GLY PHE PHE LEU          
SEQRES   3 L  445  THR ILE ILE ILE GLY ALA VAL LEU LEU MET LEU PRO ILE          
SEQRES   4 L  445  SER THR THR LYS PRO LEU SER TRP ILE ASP ALA LEU PHE          
SEQRES   5 L  445  THR ALA ALA SER ALA THR THR VAL THR GLY LEU ALA VAL          
SEQRES   6 L  445  VAL ASP THR GLY THR GLN PHE THR VAL PHE GLY GLN THR          
SEQRES   7 L  445  VAL ILE MET GLY LEU ILE GLN ILE GLY GLY LEU GLY PHE          
SEQRES   8 L  445  MET THR PHE ALA VAL LEU ILE VAL MET ILE LEU ALA ALA          
SEQRES   9 L  445  ALA ILE GLY LEU LYS GLU ARG MET LEU VAL GLN GLU ALA          
SEQRES  10 L  445  LEU ASN GLN PRO THR ILE GLY GLY VAL ILE GLY LEU VAL          
SEQRES  11 L  445  LYS VAL LEU PHE LEU PHE SER ILE SER ILE GLU LEU ILE          
SEQRES  12 L  445  ALA ALA LEU ILE LEU SER ILE ARG LEU VAL PRO GLN TYR          
SEQRES  13 L  445  GLY TRP SER SER GLY LEU PHE ALA SER LEU PHE HIS ALA          
SEQRES  14 L  445  ILE SER ALA PHE ASN ASN ALA GLY PHE SER LEU TRP PRO          
SEQRES  15 L  445  ASP ASN LEU MET SER TYR VAL GLY ASP PRO THR VAL ASN          
SEQRES  16 L  445  LEU VAL ILE THR PHE LEU PHE ILE THR GLY GLY ILE GLY          
SEQRES  17 L  445  PHE THR VAL LEU PHE ASP VAL MET LYS GLN ARG ARG PHE          
SEQRES  18 L  445  LYS THR PHE SER LEU HIS THR ALA LEU MET LEU THR GLY          
SEQRES  19 L  445  THR LEU MET LEU ASN ALA ILE ALA MET LEU THR VAL PHE          
SEQRES  20 L  445  ILE LEU GLU TYR SER ASN PRO GLY THR LEU GLY HIS LEU          
SEQRES  21 L  445  ALA ALA VAL ASP LYS LEU TRP ALA SER TYR PHE GLN ALA          
SEQRES  22 L  445  VAL THR PRO ARG THR ALA GLY PHE ASN SER LEU ASP PHE          
SEQRES  23 L  445  GLY SER MET ARG GLU GLY THR ILE VAL PHE THR LEU LEU          
SEQRES  24 L  445  LEU MET PHE ILE GLY ALA GLY SER ALA SER THR ALA SER          
SEQRES  25 L  445  GLY ILE LYS LEU THR THR PHE ILE VAL ILE LEU THR SER          
SEQRES  26 L  445  VAL ILE ALA TYR LEU ARG GLY LYS LYS GLU THR VAL ILE          
SEQRES  27 L  445  PHE ARG ARG SER ILE LYS TYR PRO ILE ILE ILE LYS ALA          
SEQRES  28 L  445  LEU ALA VAL SER VAL THR SER LEU PHE ILE VAL PHE LEU          
SEQRES  29 L  445  GLY ILE PHE ALA LEU THR ILE THR GLU GLN ALA PRO PHE          
SEQRES  30 L  445  LEU GLN ILE VAL PHE GLU THR PHE SER ALA PHE GLY THR          
SEQRES  31 L  445  VAL GLY LEU THR MET GLY LEU THR PRO GLU LEU THR THR          
SEQRES  32 L  445  ALA GLY LYS CYS ILE ILE ILE VAL ILE MET PHE ILE GLY          
SEQRES  33 L  445  ARG ILE GLY PRO LEU THR PHE VAL PHE SER PHE ALA ALA          
SEQRES  34 L  445  THR GLU GLN SER ASN ILE ARG TYR PRO ASP GLY GLU VAL          
SEQRES  35 L  445  PHE THR GLY                                                  
HET      K  I 501       1                                                       
HET      K  J 501       1                                                       
HET      K  K 501       1                                                       
HET      K  L 501       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   9    K    4(K 1+)                                                      
HELIX    1 AA1 GLY A   15  GLY A   29  1                                  15    
HELIX    2 AA2 GLU A   39  TYR A   45  1                                   7    
HELIX    3 AA3 GLU A   59  LEU A   66  1                                   8    
HELIX    4 AA4 GLY A   67  PHE A   71  5                                   5    
HELIX    5 AA5 ASN A   81  LEU A   95  1                                  15    
HELIX    6 AA6 ASN A  106  GLY A  117  1                                  12    
HELIX    7 AA7 HIS A  123  LEU A  136  1                                  14    
HELIX    8 AA8 GLY A  157  GLY A  171  1                                  15    
HELIX    9 AA9 GLU A  181  TYR A  187  1                                   7    
HELIX   10 AB1 GLU A  201  LEU A  208  1                                   8    
HELIX   11 AB2 GLY A  209  PHE A  213  5                                   5    
HELIX   12 AB3 ASN A  223  LEU A  237  1                                  15    
HELIX   13 AB4 ASN A  248  GLY A  259  1                                  12    
HELIX   14 AB5 HIS A  265  LEU A  278  1                                  14    
HELIX   15 AB6 GLY C   15  GLY C   29  1                                  15    
HELIX   16 AB7 GLU C   39  TYR C   45  1                                   7    
HELIX   17 AB8 GLU C   59  LEU C   66  1                                   8    
HELIX   18 AB9 GLY C   67  PHE C   71  5                                   5    
HELIX   19 AC1 ASN C   81  LEU C   95  1                                  15    
HELIX   20 AC2 ASN C  106  GLY C  117  1                                  12    
HELIX   21 AC3 HIS C  123  LEU C  136  1                                  14    
HELIX   22 AC4 GLY C  157  GLY C  171  1                                  15    
HELIX   23 AC5 GLU C  181  TYR C  187  1                                   7    
HELIX   24 AC6 GLU C  201  LEU C  208  1                                   8    
HELIX   25 AC7 GLY C  209  PHE C  213  5                                   5    
HELIX   26 AC8 ASN C  223  LEU C  237  1                                  15    
HELIX   27 AC9 ASN C  248  GLY C  259  1                                  12    
HELIX   28 AD1 HIS C  265  LEU C  278  1                                  14    
HELIX   29 AD2 GLY E   15  GLY E   29  1                                  15    
HELIX   30 AD3 GLU E   39  TYR E   45  1                                   7    
HELIX   31 AD4 GLU E   59  LEU E   66  1                                   8    
HELIX   32 AD5 GLY E   67  PHE E   71  5                                   5    
HELIX   33 AD6 ASN E   81  LEU E   95  1                                  15    
HELIX   34 AD7 ASN E  106  GLY E  117  1                                  12    
HELIX   35 AD8 HIS E  123  LEU E  136  1                                  14    
HELIX   36 AD9 GLY E  157  GLY E  171  1                                  15    
HELIX   37 AE1 GLU E  181  TYR E  187  1                                   7    
HELIX   38 AE2 GLU E  201  LEU E  208  1                                   8    
HELIX   39 AE3 GLY E  209  PHE E  213  5                                   5    
HELIX   40 AE4 ASN E  223  LEU E  237  1                                  15    
HELIX   41 AE5 ASN E  248  GLY E  259  1                                  12    
HELIX   42 AE6 HIS E  265  LEU E  278  1                                  14    
HELIX   43 AE7 GLY G   15  GLY G   29  1                                  15    
HELIX   44 AE8 GLU G   39  TYR G   45  1                                   7    
HELIX   45 AE9 GLU G   59  SER G   65  1                                   7    
HELIX   46 AF1 GLY G   67  PHE G   71  5                                   5    
HELIX   47 AF2 ASN G   81  LEU G   95  1                                  15    
HELIX   48 AF3 ASN G  106  GLY G  117  1                                  12    
HELIX   49 AF4 HIS G  123  LEU G  136  1                                  14    
HELIX   50 AF5 GLY G  157  GLY G  171  1                                  15    
HELIX   51 AF6 GLU G  181  TYR G  187  1                                   7    
HELIX   52 AF7 GLU G  201  LEU G  208  1                                   8    
HELIX   53 AF8 GLY G  209  PHE G  213  5                                   5    
HELIX   54 AF9 ASN G  223  LEU G  237  1                                  15    
HELIX   55 AG1 ASN G  248  GLY G  259  1                                  12    
HELIX   56 AG2 HIS G  265  LEU G  278  1                                  14    
HELIX   57 AG3 PRO I   16  LEU I   35  1                                  20    
HELIX   58 AG4 PHE I   52  THR I   59  1                                   8    
HELIX   59 AG5 THR I   78  GLY I   87  1                                  10    
HELIX   60 AG6 GLY I  128  ALA I  144  1                                  17    
HELIX   61 AG7 VAL I  153  GLY I  157  5                                   5    
HELIX   62 AG8 PHE I  163  HIS I  168  1                                   6    
HELIX   63 AG9 HIS I  168  PHE I  173  1                                   6    
HELIX   64 AH1 ASP I  191  GLY I  205  1                                  15    
HELIX   65 AH2 GLY I  208  GLN I  218  1                                  11    
HELIX   66 AH3 SER I  225  GLU I  250  1                                  26    
HELIX   67 AH4 LYS I  265  ALA I  273  1                                   9    
HELIX   68 AH5 ASP I  285  MET I  289  5                                   5    
HELIX   69 AH6 ARG I  290  ILE I  303  1                                  14    
HELIX   70 AH7 LYS I  315  LEU I  330  1                                  16    
HELIX   71 AH8 LYS I  344  ILE I  371  1                                  28    
HELIX   72 AH9 PRO I  376  GLY I  389  1                                  14    
HELIX   73 AI1 THR I  403  ILE I  418  1                                  16    
HELIX   74 AI2 GLY I  419  PHE I  425  1                                   7    
HELIX   75 AI3 PRO J   16  LEU J   35  1                                  20    
HELIX   76 AI4 PHE J   52  THR J   59  1                                   8    
HELIX   77 AI5 THR J   78  GLY J   87  1                                  10    
HELIX   78 AI6 GLY J  128  ALA J  144  1                                  17    
HELIX   79 AI7 VAL J  153  GLY J  157  5                                   5    
HELIX   80 AI8 PHE J  163  HIS J  168  1                                   6    
HELIX   81 AI9 HIS J  168  PHE J  173  1                                   6    
HELIX   82 AJ1 ASP J  191  GLY J  205  1                                  15    
HELIX   83 AJ2 GLY J  208  GLN J  218  1                                  11    
HELIX   84 AJ3 SER J  225  GLU J  250  1                                  26    
HELIX   85 AJ4 LYS J  265  ALA J  273  1                                   9    
HELIX   86 AJ5 ASP J  285  MET J  289  5                                   5    
HELIX   87 AJ6 ARG J  290  ILE J  303  1                                  14    
HELIX   88 AJ7 LYS J  315  LEU J  330  1                                  16    
HELIX   89 AJ8 TYR J  345  ILE J  371  1                                  27    
HELIX   90 AJ9 PRO J  376  GLY J  389  1                                  14    
HELIX   91 AK1 THR J  403  ILE J  418  1                                  16    
HELIX   92 AK2 GLY J  419  PHE J  425  1                                   7    
HELIX   93 AK3 PRO K   16  LEU K   35  1                                  20    
HELIX   94 AK4 PHE K   52  THR K   59  1                                   8    
HELIX   95 AK5 THR K   78  GLY K   87  1                                  10    
HELIX   96 AK6 GLY K  128  ALA K  144  1                                  17    
HELIX   97 AK7 VAL K  153  GLY K  157  5                                   5    
HELIX   98 AK8 HIS K  168  PHE K  173  1                                   6    
HELIX   99 AK9 ASP K  191  GLY K  205  1                                  15    
HELIX  100 AL1 GLY K  208  GLN K  218  1                                  11    
HELIX  101 AL2 SER K  225  GLU K  250  1                                  26    
HELIX  102 AL3 LYS K  265  ALA K  273  1                                   9    
HELIX  103 AL4 ASP K  285  MET K  289  5                                   5    
HELIX  104 AL5 ARG K  290  ILE K  303  1                                  14    
HELIX  105 AL6 LYS K  315  LEU K  330  1                                  16    
HELIX  106 AL7 TYR K  345  ILE K  371  1                                  27    
HELIX  107 AL8 PRO K  376  GLY K  389  1                                  14    
HELIX  108 AL9 THR K  403  ILE K  418  1                                  16    
HELIX  109 AM1 GLY K  419  PHE K  425  1                                   7    
HELIX  110 AM2 PRO L   16  LEU L   35  1                                  20    
HELIX  111 AM3 PHE L   52  THR L   59  1                                   8    
HELIX  112 AM4 THR L   78  GLY L   87  1                                  10    
HELIX  113 AM5 GLY L  128  ALA L  144  1                                  17    
HELIX  114 AM6 VAL L  153  GLY L  157  5                                   5    
HELIX  115 AM7 PHE L  163  HIS L  168  1                                   6    
HELIX  116 AM8 HIS L  168  PHE L  173  1                                   6    
HELIX  117 AM9 ASP L  191  ILE L  207  1                                  17    
HELIX  118 AN1 GLY L  208  GLN L  218  1                                  11    
HELIX  119 AN2 SER L  225  GLU L  250  1                                  26    
HELIX  120 AN3 LYS L  265  ALA L  273  1                                   9    
HELIX  121 AN4 ASP L  285  MET L  289  5                                   5    
HELIX  122 AN5 ARG L  290  ILE L  303  1                                  14    
HELIX  123 AN6 LYS L  315  LEU L  330  1                                  16    
HELIX  124 AN7 LYS L  344  ILE L  371  1                                  28    
HELIX  125 AN8 PRO L  376  GLY L  389  1                                  14    
HELIX  126 AN9 THR L  403  ILE L  418  1                                  16    
HELIX  127 AO1 GLY L  419  PHE L  425  1                                   7    
SHEET    1 AA1 4 PHE A   9  ILE A  12  0                                        
SHEET    2 AA1 4 TYR A  73  VAL A  76  1  O  ILE A  75   N  ILE A  12           
SHEET    3 AA1 4 ASN A  99  LYS A 103  1  O  TRP A 101   N  VAL A  74           
SHEET    4 AA1 4 ARG A 120  ILE A 122  1  O  ARG A 120   N  VAL A 102           
SHEET    1 AA2 2 VAL A  35  ASP A  36  0                                        
SHEET    2 AA2 2 VAL A  53  ILE A  54  1  O  VAL A  53   N  ASP A  36           
SHEET    1 AA3 4 PHE A 151  ILE A 154  0                                        
SHEET    2 AA3 4 TYR A 215  VAL A 218  1  O  ILE A 217   N  ILE A 154           
SHEET    3 AA3 4 ASN A 241  LYS A 245  1  O  TRP A 243   N  VAL A 216           
SHEET    4 AA3 4 ARG A 262  ILE A 264  1  O  ARG A 262   N  VAL A 244           
SHEET    1 AA4 2 VAL A 177  ASP A 178  0                                        
SHEET    2 AA4 2 VAL A 195  ILE A 196  1  O  VAL A 195   N  ASP A 178           
SHEET    1 AA5 4 PHE C   9  ILE C  12  0                                        
SHEET    2 AA5 4 TYR C  73  VAL C  76  1  O  ILE C  75   N  ILE C  12           
SHEET    3 AA5 4 ASN C  99  LYS C 103  1  O  TRP C 101   N  VAL C  74           
SHEET    4 AA5 4 ARG C 120  ILE C 122  1  O  ARG C 120   N  VAL C 102           
SHEET    1 AA6 2 VAL C  35  ASP C  36  0                                        
SHEET    2 AA6 2 VAL C  53  ILE C  54  1  O  VAL C  53   N  ASP C  36           
SHEET    1 AA7 4 PHE C 151  ILE C 154  0                                        
SHEET    2 AA7 4 TYR C 215  VAL C 218  1  O  ILE C 217   N  ILE C 154           
SHEET    3 AA7 4 ASN C 241  LYS C 245  1  O  TRP C 243   N  VAL C 216           
SHEET    4 AA7 4 ARG C 262  ILE C 264  1  O  ARG C 262   N  VAL C 244           
SHEET    1 AA8 2 VAL C 177  ASP C 178  0                                        
SHEET    2 AA8 2 VAL C 195  ILE C 196  1  O  VAL C 195   N  ASP C 178           
SHEET    1 AA9 4 PHE E   9  ILE E  12  0                                        
SHEET    2 AA9 4 TYR E  73  VAL E  76  1  O  ILE E  75   N  ILE E  12           
SHEET    3 AA9 4 ASN E  99  LYS E 103  1  O  TRP E 101   N  VAL E  74           
SHEET    4 AA9 4 ARG E 120  ILE E 122  1  O  ARG E 120   N  VAL E 102           
SHEET    1 AB1 2 VAL E  35  ASP E  36  0                                        
SHEET    2 AB1 2 VAL E  53  ILE E  54  1  O  VAL E  53   N  ASP E  36           
SHEET    1 AB2 4 PHE E 151  ILE E 154  0                                        
SHEET    2 AB2 4 TYR E 215  VAL E 218  1  O  ILE E 217   N  ILE E 154           
SHEET    3 AB2 4 ASN E 241  LYS E 245  1  O  TRP E 243   N  VAL E 216           
SHEET    4 AB2 4 ARG E 262  ILE E 264  1  O  ARG E 262   N  VAL E 244           
SHEET    1 AB3 2 VAL E 177  ASP E 178  0                                        
SHEET    2 AB3 2 VAL E 195  ILE E 196  1  O  VAL E 195   N  ASP E 178           
SHEET    1 AB4 4 PHE G   9  ILE G  12  0                                        
SHEET    2 AB4 4 TYR G  73  VAL G  76  1  O  ILE G  75   N  ILE G  12           
SHEET    3 AB4 4 ASN G  99  LYS G 103  1  O  TRP G 101   N  VAL G  74           
SHEET    4 AB4 4 ARG G 120  ILE G 122  1  O  ARG G 120   N  VAL G 102           
SHEET    1 AB5 2 VAL G  35  ASP G  36  0                                        
SHEET    2 AB5 2 VAL G  53  ILE G  54  1  O  VAL G  53   N  ASP G  36           
SHEET    1 AB6 6 VAL G 195  ILE G 196  0                                        
SHEET    2 AB6 6 VAL G 174  ASP G 178  1  N  ALA G 176   O  VAL G 195           
SHEET    3 AB6 6 PHE G 151  ILE G 154  1  N  PHE G 151   O  LEU G 175           
SHEET    4 AB6 6 TYR G 215  VAL G 218  1  O  ILE G 217   N  ILE G 154           
SHEET    5 AB6 6 ASN G 241  LYS G 245  1  O  TRP G 243   N  VAL G 216           
SHEET    6 AB6 6 ARG G 262  ILE G 264  1  O  ARG G 262   N  VAL G 244           
LINK         O   THR I  61                 K     K I 501     1555   1555  3.00  
LINK         O   ASN I 175                 K     K I 501     1555   1555  3.49  
LINK         O   ALA I 176                 K     K I 501     1555   1555  3.06  
LINK         O   THR I 278                 K     K I 501     1555   1555  3.42  
LINK         O   ALA I 279                 K     K I 501     1555   1555  3.39  
LINK         O   THR I 390                 K     K I 501     1555   1555  3.16  
LINK         O   VAL I 391                 K     K I 501     1555   1555  3.33  
LINK         O   VAL J  60                 K     K J 501     1555   1555  3.07  
LINK         O   THR J  61                 K     K J 501     1555   1555  3.06  
LINK         O   ASN J 175                 K     K J 501     1555   1555  3.25  
LINK         O   ALA J 176                 K     K J 501     1555   1555  3.18  
LINK         O   THR J 278                 K     K J 501     1555   1555  3.47  
LINK         O   THR J 390                 K     K J 501     1555   1555  3.03  
LINK         O   ASN K 175                 K     K K 501     1555   1555  3.38  
LINK         O   THR K 278                 K     K K 501     1555   1555  2.92  
LINK         O   ALA K 279                 K     K K 501     1555   1555  3.47  
LINK         O   THR K 390                 K     K K 501     1555   1555  3.04  
LINK         O   VAL K 391                 K     K K 501     1555   1555  3.38  
LINK         O   VAL L  60                 K     K L 501     1555   1555  2.92  
LINK         O   THR L  61                 K     K L 501     1555   1555  3.14  
LINK         O   ASN L 175                 K     K L 501     1555   1555  3.09  
LINK         O   ALA L 176                 K     K L 501     1555   1555  3.17  
LINK         O   THR L 278                 K     K L 501     1555   1555  3.47  
LINK         O   THR L 390                 K     K L 501     1555   1555  2.96  
SITE     1 AC1  9 VAL I  60  THR I  61  ASN I 175  ALA I 176                    
SITE     2 AC1  9 THR I 278  ALA I 279  THR I 390  VAL I 391                    
SITE     3 AC1  9 GLY I 392                                                     
SITE     1 AC2  7 VAL J  60  THR J  61  ASN J 175  ALA J 176                    
SITE     2 AC2  7 THR J 278  THR J 390  VAL J 391                               
SITE     1 AC3  8 THR K  61  ASN K 175  ALA K 176  THR K 278                    
SITE     2 AC3  8 ALA K 279  GLY K 280  THR K 390  VAL K 391                    
SITE     1 AC4  6 VAL L  60  THR L  61  ASN L 175  ALA L 176                    
SITE     2 AC4  6 THR L 278  THR L 390                                          
CRYST1  307.060   79.410  205.650  90.00  98.10  90.00 C 1 2 1      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      0.003257  0.000000  0.000463        0.00000                         
SCALE2      0.000000  0.012593  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004912        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system