GenomeNet

Database: PDB
Entry: 1Q43
LinkDB: 1Q43
Original site: 1Q43 
HEADER    TRANSPORT PROTEIN                       01-AUG-03   1Q43              
TITLE     HCN2I 443-640 IN THE PRESENCE OF CAMP, SELENOMETHIONINE DERIVATIVE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC        
COMPND   3 NUCLEOTIDE-GATED CHANNEL 2;                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: RESIDUES 443-645;                                          
COMPND   6 SYNONYM: BRAIN CYCLIC NUCLEOTIDE GATED CHANNEL 2, BCNG-2,            
COMPND   7 HYPERPOLARIZATION-ACTIVATED CATION CHANNEL 1, HAC-1;                 
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 GENE: HCN2, BCNG2 OR HAC1;                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);                               
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PETGQ                                     
KEYWDS    CNBD, C-LINKER, PACEMAKER, HCN,HCN2, CHANNEL, CYCLIC NUCLEOTIDE, CAP, 
KEYWDS   2 PKA, CAMP, ION CHANNEL, LIGAND, TRANSPORT PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.N.ZAGOTTA,N.B.OLIVIER,K.D.BLACK,E.C.YOUNG,R.OLSON,J.E.GOUAUX        
REVDAT   3   13-JUL-11 1Q43    1       VERSN                                    
REVDAT   2   24-FEB-09 1Q43    1       VERSN                                    
REVDAT   1   09-SEP-03 1Q43    0                                                
JRNL        AUTH   W.N.ZAGOTTA,N.B.OLIVIER,K.D.BLACK,E.C.YOUNG,R.OLSON,         
JRNL        AUTH 2 J.E.GOUAUX                                                   
JRNL        TITL   STRUCTURAL BASIS FOR MODULATION AND AGONIST SPECIFICITY OF   
JRNL        TITL 2 HCN PACEMAKER CHANNELS                                       
JRNL        REF    NATURE                        V. 425   200 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12968185                                                     
JRNL        DOI    10.1038/NATURE01922                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.81                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 31762                          
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) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3186                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE                    : 0.2330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 619                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2997                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 485                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.81000                                              
REMARK   3    B22 (A**2) : 1.81000                                              
REMARK   3    B33 (A**2) : -3.63000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.05                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
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) : 1.290 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.830 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.627 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.061 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CMPCNS.PARAM                                   
REMARK   3  PARAMETER FILE  4  : 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                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q43 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019890.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979493,0.979184,0.934038         
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31762                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: RESOLVE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, SODIUM CITRATE, SODIUM          
REMARK 280  CHLORIDE, DTT, HEPES, CAMP, PH 4.6, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       47.37500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.37500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.21000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.37500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.37500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.21000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       47.37500            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       47.37500            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       62.21000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       47.37500            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       47.37500            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       62.21000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 ONE PROTMER. THERE ARE TWO DISTINCT PROTOMERS IN THE ASYMMETRIC      
REMARK 300 UNIT LABELED A & B. EACH PROTOMER ASSOCIATES WITH ITS LIKE TO FORM   
REMARK 300 THE TETRAMER. TO GENERATE THE TETRAMER APPLY THE FOLLOWING SYMMETRY  
REMARK 300 OPERATIONS TO THE ASYMMETRIC UNIT: 1-Y,X,Z AND Y,1-X,Z AND 1-X,1-Y,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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 11420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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       94.75000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       94.75000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       94.75000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       94.75000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 26440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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       94.75000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       94.75000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       94.75000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       94.75000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000       47.37500            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000       47.37500            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000      -62.21000            
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000       47.37500            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000       47.37500            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000      -62.21000            
REMARK 350   BIOMT1   7  0.000000 -1.000000  0.000000       47.37500            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000       47.37500            
REMARK 350   BIOMT3   7  0.000000  0.000000  1.000000      -62.21000            
REMARK 350   BIOMT1   8  0.000000  1.000000  0.000000       47.37500            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000       47.37500            
REMARK 350   BIOMT3   8  0.000000  0.000000  1.000000      -62.21000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   439                                                      
REMARK 465     SER A   440                                                      
REMARK 465     ALA A   441                                                      
REMARK 465     MET A   442                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     GLY A   568                                                      
REMARK 465     ASN A   569                                                      
REMARK 465     LYS A   570                                                      
REMARK 465     ILE A   636                                                      
REMARK 465     GLY A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     LYS A   639                                                      
REMARK 465     ASN A   640                                                      
REMARK 465     SER A   641                                                      
REMARK 465     ILE A   642                                                      
REMARK 465     LEU A   643                                                      
REMARK 465     LEU A   644                                                      
REMARK 465     HIS A   645                                                      
REMARK 465     GLY B   439                                                      
REMARK 465     SER B   440                                                      
REMARK 465     ALA B   441                                                      
REMARK 465     MET B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     SER B   444                                                      
REMARK 465     LYS B   567                                                      
REMARK 465     GLY B   568                                                      
REMARK 465     ASN B   569                                                      
REMARK 465     LYS B   570                                                      
REMARK 465     GLY B   637                                                      
REMARK 465     LYS B   638                                                      
REMARK 465     LYS B   639                                                      
REMARK 465     ASN B   640                                                      
REMARK 465     SER B   641                                                      
REMARK 465     ILE B   642                                                      
REMARK 465     LEU B   643                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     HIS B   645                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 443    CG   OD1  OD2                                       
REMARK 470     SER A 444    OG                                                  
REMARK 470     LYS A 454    CG   CD   CE   NZ                                   
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     SER A 461    OG                                                  
REMARK 470     ASP A 468    CG   OD1  OD2                                       
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     GLU A 488    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 534    CG   CD   CE   NZ                                   
REMARK 470     LYS A 552    CG   CD   CE   NZ                                   
REMARK 470     LYS A 553    CG   CD   CE   NZ                                   
REMARK 470     GLN A 558    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 565    CG   CD1  CD2                                       
REMARK 470     GLU A 571    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 573    CG   CD   CE   NZ                                   
REMARK 470     ASP A 634    CG   OD1  OD2                                       
REMARK 470     ARG B 447    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 448    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 450    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 452    CG   CD   CE   NZ                                   
REMARK 470     LYS B 454    CG   CD   CE   NZ                                   
REMARK 470     ASP B 468    CG   OD1  OD2                                       
REMARK 470     GLU B 478    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 484    CG   CD   CE   NZ                                   
REMARK 470     ASP B 489    CG   OD1  OD2                                       
REMARK 470     GLU B 502    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 510    CG   CD   CE   NZ                                   
REMARK 470     LYS B 534    CG   CD   CE   NZ                                   
REMARK 470     LYS B 552    CG   CD   CE   NZ                                   
REMARK 470     THR B 566    OG1  CG2                                            
REMARK 470     GLU B 571    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 636    CG1  CG2  CD1                                       
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    ASP A 576      129.79    -36.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 731        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH A 808        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A 828        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 839        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 841        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 848        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH A 864        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 865        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH A 869        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 771        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B 820        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH B 826        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH B 829        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B 831        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH B 845        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B 853        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B 855        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH B 863        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 881        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH B 884        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B 894        DISTANCE =  9.27 ANGSTROMS                       
REMARK 525    HOH B 895        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH B 900        DISTANCE =  7.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 646                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP B 646                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Q3E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Q5O   RELATED DB: PDB                                   
DBREF  1Q43 A  443   645  UNP    O88703   HCN2_MOUSE     443    645             
DBREF  1Q43 B  443   645  UNP    O88703   HCN2_MOUSE     443    645             
SEQADV 1Q43 GLY A  439  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 SER A  440  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 ALA A  441  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 MET A  442  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 MSE A  460  UNP  O88703    MET   460 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  485  UNP  O88703    MET   485 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  515  UNP  O88703    MET   515 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  529  UNP  O88703    MET   529 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  554  UNP  O88703    MET   554 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  572  UNP  O88703    MET   572 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  620  UNP  O88703    MET   620 MODIFIED RESIDUE               
SEQADV 1Q43 MSE A  621  UNP  O88703    MET   621 MODIFIED RESIDUE               
SEQADV 1Q43 GLY B  439  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 SER B  440  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 ALA B  441  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 MET B  442  UNP  O88703              CLONING ARTIFACT               
SEQADV 1Q43 MSE B  460  UNP  O88703    MET   460 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  485  UNP  O88703    MET   485 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  515  UNP  O88703    MET   515 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  529  UNP  O88703    MET   529 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  554  UNP  O88703    MET   554 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  572  UNP  O88703    MET   572 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  620  UNP  O88703    MET   620 MODIFIED RESIDUE               
SEQADV 1Q43 MSE B  621  UNP  O88703    MET   621 MODIFIED RESIDUE               
SEQRES   1 A  207  GLY SER ALA MET ASP SER SER ARG ARG GLN TYR GLN GLU          
SEQRES   2 A  207  LYS TYR LYS GLN VAL GLU GLN TYR MSE SER PHE HIS LYS          
SEQRES   3 A  207  LEU PRO ALA ASP PHE ARG GLN LYS ILE HIS ASP TYR TYR          
SEQRES   4 A  207  GLU HIS ARG TYR GLN GLY LYS MSE PHE ASP GLU ASP SER          
SEQRES   5 A  207  ILE LEU GLY GLU LEU ASN GLY PRO LEU ARG GLU GLU ILE          
SEQRES   6 A  207  VAL ASN PHE ASN CYS ARG LYS LEU VAL ALA SER MSE PRO          
SEQRES   7 A  207  LEU PHE ALA ASN ALA ASP PRO ASN PHE VAL THR ALA MSE          
SEQRES   8 A  207  LEU THR LYS LEU LYS PHE GLU VAL PHE GLN PRO GLY ASP          
SEQRES   9 A  207  TYR ILE ILE ARG GLU GLY THR ILE GLY LYS LYS MSE TYR          
SEQRES  10 A  207  PHE ILE GLN HIS GLY VAL VAL SER VAL LEU THR LYS GLY          
SEQRES  11 A  207  ASN LYS GLU MSE LYS LEU SER ASP GLY SER TYR PHE GLY          
SEQRES  12 A  207  GLU ILE CYS LEU LEU THR ARG GLY ARG ARG THR ALA SER          
SEQRES  13 A  207  VAL ARG ALA ASP THR TYR CYS ARG LEU TYR SER LEU SER          
SEQRES  14 A  207  VAL ASP ASN PHE ASN GLU VAL LEU GLU GLU TYR PRO MSE          
SEQRES  15 A  207  MSE ARG ARG ALA PHE GLU THR VAL ALA ILE ASP ARG LEU          
SEQRES  16 A  207  ASP ARG ILE GLY LYS LYS ASN SER ILE LEU LEU HIS              
SEQRES   1 B  207  GLY SER ALA MET ASP SER SER ARG ARG GLN TYR GLN GLU          
SEQRES   2 B  207  LYS TYR LYS GLN VAL GLU GLN TYR MSE SER PHE HIS LYS          
SEQRES   3 B  207  LEU PRO ALA ASP PHE ARG GLN LYS ILE HIS ASP TYR TYR          
SEQRES   4 B  207  GLU HIS ARG TYR GLN GLY LYS MSE PHE ASP GLU ASP SER          
SEQRES   5 B  207  ILE LEU GLY GLU LEU ASN GLY PRO LEU ARG GLU GLU ILE          
SEQRES   6 B  207  VAL ASN PHE ASN CYS ARG LYS LEU VAL ALA SER MSE PRO          
SEQRES   7 B  207  LEU PHE ALA ASN ALA ASP PRO ASN PHE VAL THR ALA MSE          
SEQRES   8 B  207  LEU THR LYS LEU LYS PHE GLU VAL PHE GLN PRO GLY ASP          
SEQRES   9 B  207  TYR ILE ILE ARG GLU GLY THR ILE GLY LYS LYS MSE TYR          
SEQRES  10 B  207  PHE ILE GLN HIS GLY VAL VAL SER VAL LEU THR LYS GLY          
SEQRES  11 B  207  ASN LYS GLU MSE LYS LEU SER ASP GLY SER TYR PHE GLY          
SEQRES  12 B  207  GLU ILE CYS LEU LEU THR ARG GLY ARG ARG THR ALA SER          
SEQRES  13 B  207  VAL ARG ALA ASP THR TYR CYS ARG LEU TYR SER LEU SER          
SEQRES  14 B  207  VAL ASP ASN PHE ASN GLU VAL LEU GLU GLU TYR PRO MSE          
SEQRES  15 B  207  MSE ARG ARG ALA PHE GLU THR VAL ALA ILE ASP ARG LEU          
SEQRES  16 B  207  ASP ARG ILE GLY LYS LYS ASN SER ILE LEU LEU HIS              
MODRES 1Q43 MSE A  460  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  485  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  515  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  529  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  554  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  572  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  620  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE A  621  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  460  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  485  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  515  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  529  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  554  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  572  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  620  MET  SELENOMETHIONINE                                   
MODRES 1Q43 MSE B  621  MET  SELENOMETHIONINE                                   
HET    MSE  A 460       8                                                       
HET    MSE  A 485       8                                                       
HET    MSE  A 515       8                                                       
HET    MSE  A 529       8                                                       
HET    MSE  A 554       8                                                       
HET    MSE  A 572       8                                                       
HET    MSE  A 620       8                                                       
HET    MSE  A 621       8                                                       
HET    MSE  B 460       8                                                       
HET    MSE  B 485       8                                                       
HET    MSE  B 515       8                                                       
HET    MSE  B 529       8                                                       
HET    MSE  B 554       8                                                       
HET    MSE  B 572       8                                                       
HET    MSE  B 620       8                                                       
HET    MSE  B 621       8                                                       
HET    CMP  A 646      22                                                       
HET    CMP  B 646      22                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE                             
HETSYN     CMP CYCLIC AMP; CAMP                                                 
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  CMP    2(C10 H12 N5 O6 P)                                           
FORMUL   5  HOH   *485(H2 O)                                                    
HELIX    1   1 ASP A  443  HIS A  463  1                                  21    
HELIX    2   2 PRO A  466  GLN A  482  1                                  17    
HELIX    3   3 ASP A  487  LEU A  495  1                                   9    
HELIX    4   4 ASN A  496  CYS A  508  1                                  13    
HELIX    5   5 CYS A  508  SER A  514  1                                   7    
HELIX    6   6 MSE A  515  ASN A  520  1                                   6    
HELIX    7   7 ASP A  522  LEU A  533  1                                  12    
HELIX    8   8 GLY A  581  ARG A  588  1                                   8    
HELIX    9   9 VAL A  608  TYR A  618  1                                  11    
HELIX   10  10 MSE A  621  ARG A  635  1                                  15    
HELIX   11  11 SER B  445  HIS B  463  1                                  19    
HELIX   12  12 PRO B  466  GLN B  482  1                                  17    
HELIX   13  13 ASP B  487  LEU B  495  1                                   9    
HELIX   14  14 ASN B  496  CYS B  508  1                                  13    
HELIX   15  15 CYS B  508  SER B  514  1                                   7    
HELIX   16  16 MSE B  515  ASN B  520  1                                   6    
HELIX   17  17 ASP B  522  LEU B  533  1                                  12    
HELIX   18  18 GLY B  581  ARG B  588  1                                   8    
HELIX   19  19 VAL B  608  TYR B  618  1                                  11    
HELIX   20  20 MSE B  621  ARG B  635  1                                  15    
SHEET    1   A 4 LYS A 534  PHE A 538  0                                        
SHEET    2   A 4 CYS A 601  SER A 607 -1  O  LEU A 603   N  GLU A 536           
SHEET    3   A 4 LYS A 553  HIS A 559 -1  N  HIS A 559   O  ARG A 602           
SHEET    4   A 4 TYR A 579  PHE A 580 -1  O  PHE A 580   N  TYR A 555           
SHEET    1   B 4 TYR A 543  ILE A 545  0                                        
SHEET    2   B 4 SER A 594  ALA A 597 -1  O  VAL A 595   N  ILE A 545           
SHEET    3   B 4 VAL A 562  LEU A 565 -1  N  LEU A 565   O  SER A 594           
SHEET    4   B 4 MSE A 572  LEU A 574 -1  O  MSE A 572   N  VAL A 564           
SHEET    1   C 4 LYS B 534  PHE B 538  0                                        
SHEET    2   C 4 CYS B 601  SER B 607 -1  O  LEU B 603   N  GLU B 536           
SHEET    3   C 4 LYS B 553  HIS B 559 -1  N  HIS B 559   O  ARG B 602           
SHEET    4   C 4 TYR B 579  PHE B 580 -1  O  PHE B 580   N  TYR B 555           
SHEET    1   D 4 TYR B 543  ILE B 545  0                                        
SHEET    2   D 4 SER B 594  ALA B 597 -1  O  VAL B 595   N  ILE B 545           
SHEET    3   D 4 VAL B 562  LEU B 565 -1  N  SER B 563   O  ARG B 596           
SHEET    4   D 4 MSE B 572  LEU B 574 -1  O  MSE B 572   N  VAL B 564           
LINK         C   TYR A 459                 N   MSE A 460     1555   1555  1.33  
LINK         C   MSE A 460                 N   SER A 461     1555   1555  1.33  
LINK         C   LYS A 484                 N   MSE A 485     1555   1555  1.33  
LINK         C   MSE A 485                 N   PHE A 486     1555   1555  1.33  
LINK         C   SER A 514                 N   MSE A 515     1555   1555  1.33  
LINK         C   MSE A 515                 N   PRO A 516     1555   1555  1.34  
LINK         C   ALA A 528                 N   MSE A 529     1555   1555  1.33  
LINK         C   MSE A 529                 N   LEU A 530     1555   1555  1.33  
LINK         C   LYS A 553                 N   MSE A 554     1555   1555  1.33  
LINK         C   MSE A 554                 N   TYR A 555     1555   1555  1.33  
LINK         C   GLU A 571                 N   MSE A 572     1555   1555  1.33  
LINK         C   MSE A 572                 N   LYS A 573     1555   1555  1.33  
LINK         C   PRO A 619                 N   MSE A 620     1555   1555  1.33  
LINK         C   MSE A 620                 N   MSE A 621     1555   1555  1.33  
LINK         C   MSE A 621                 N   ARG A 622     1555   1555  1.33  
LINK         C   TYR B 459                 N   MSE B 460     1555   1555  1.33  
LINK         C   MSE B 460                 N   SER B 461     1555   1555  1.33  
LINK         C   LYS B 484                 N   MSE B 485     1555   1555  1.33  
LINK         C   MSE B 485                 N   PHE B 486     1555   1555  1.33  
LINK         C   SER B 514                 N   MSE B 515     1555   1555  1.33  
LINK         C   MSE B 515                 N   PRO B 516     1555   1555  1.34  
LINK         C   ALA B 528                 N   MSE B 529     1555   1555  1.33  
LINK         C   MSE B 529                 N   LEU B 530     1555   1555  1.33  
LINK         C   LYS B 553                 N   MSE B 554     1555   1555  1.33  
LINK         C   MSE B 554                 N   TYR B 555     1555   1555  1.33  
LINK         C   GLU B 571                 N   MSE B 572     1555   1555  1.33  
LINK         C   MSE B 572                 N   LYS B 573     1555   1555  1.33  
LINK         C   PRO B 619                 N   MSE B 620     1555   1555  1.33  
LINK         C   MSE B 620                 N   MSE B 621     1555   1555  1.33  
LINK         C   MSE B 621                 N   ARG B 622     1555   1555  1.33  
SITE     1 AC1 11 VAL A 564  MSE A 572  PHE A 580  GLY A 581                    
SITE     2 AC1 11 GLU A 582  ILE A 583  CYS A 584  ARG A 591                    
SITE     3 AC1 11 THR A 592  ALA A 593  ARG A 632                               
SITE     1 AC2 11 VAL B 564  MSE B 572  PHE B 580  GLY B 581                    
SITE     2 AC2 11 GLU B 582  ILE B 583  CYS B 584  ARG B 591                    
SITE     3 AC2 11 THR B 592  ALA B 593  ARG B 632                               
CRYST1   94.750   94.750  124.420  90.00  90.00  90.00 I 4          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      0.010554  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010554  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008037        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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