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Database: PDB
Entry: 5KHH
LinkDB: 5KHH
Original site: 5KHH 
HEADER    TRANSPORT PROTEIN                       14-JUN-16   5KHH              
TITLE     HCN2 CNBD IN COMPLEX WITH INOSINE-3', 5'-CYCLIC MONOPHOSPHATE (CIMP)  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC        
COMPND   3 NUCLEOTIDE-GATED CHANNEL 2;                                          
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 443-643;                                      
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: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: HCN2, BCNG2, HAC1;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASIMD;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    PROTEIN-LIGAND COMPLEX, CYCILC NUCLEOTIDE BINDING DOMAIN, ION         
KEYWDS   2 TRANSPORT, TRANSPORT PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.C.T.NG,I.PUTRENKO,V.BARONAS,F.VAN PETEGEM,E.A.ACCILI                
REVDAT   2   19-OCT-16 5KHH    1       JRNL                                     
REVDAT   1   14-SEP-16 5KHH    0                                                
JRNL        AUTH   L.C.NG,I.PUTRENKO,V.BARONAS,F.VAN PETEGEM,E.A.ACCILI         
JRNL        TITL   CYCLIC PURINE AND PYRIMIDINE NUCLEOTIDES BIND TO THE HCN2    
JRNL        TITL 2 ION CHANNEL AND VARIABLY PROMOTE C-TERMINAL DOMAIN           
JRNL        TITL 3 INTERACTIONS AND OPENING.                                    
JRNL        REF    STRUCTURE                     V.  24  1629 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27568927                                                     
JRNL        DOI    10.1016/J.STR.2016.06.024                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24442                          
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 + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1711                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.4610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1571                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 165                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.76                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.738         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1680 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1554 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2277 ; 1.496 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3566 ; 0.792 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   206 ; 4.842 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;30.398 ;23.012       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   288 ;14.997 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;13.671 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   241 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1926 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   415 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MOLECULAR REPLACEMENT                     
REMARK   4                                                                      
REMARK   4 5KHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222235.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979440                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : 1000 UM THICK SENSOR               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26044                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 9.830                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.14700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 1Q5O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NACL, 0.1 MM SODIUM CITRATE PH    
REMARK 280  5.5, 14.5% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       48.01850            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       57.95650            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       48.01850            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       57.95650            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       48.01850            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       57.95650            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       48.01850            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       57.95650            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       48.01850            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       57.95650            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       48.01850            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       57.95650            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       48.01850            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       57.95650            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       48.01850            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       48.01850            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       57.95650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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        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     SER A   440                                                      
REMARK 465     ASN A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     ASP A   443                                                      
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 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     SER A 444    OG                                                  
REMARK 470     ARG A 447    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 448    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 454    CG   CD   CE   NZ                                   
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     LYS A 534    CG   CD   CE   NZ                                   
REMARK 470     LYS A 567    CG   CD   CE   NZ                                   
REMARK 470     ASN A 569    CG   OD1  ND2                                       
REMARK 470     LYS A 570    CG   CD   CE   NZ                                   
REMARK 470     LYS A 638    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   502     O    HOH A   801              1.81            
REMARK 500   O    ASN A   520     O    HOH A   802              2.12            
REMARK 500   O    HOH A   802     O    HOH A   932              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   801     O    HOH A   895     3555     1.96            
REMARK 500   O    HOH A   815     O    HOH A   913    13444     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    MET A 460   CG  -  SD  -  CE  ANGL. DEV. = -17.6 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    LYS A 567      -64.24     -9.23                                   
REMARK 500    ASN A 569       17.71   -147.91                                   
REMARK 500    LYS A 570      116.46     73.47                                   
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 966        DISTANCE =  6.72 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6SW A 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KHG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KHI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KHJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KHK   RELATED DB: PDB                                   
DBREF  5KHH A  443   643  UNP    O88703   HCN2_MOUSE     443    643             
SEQADV 5KHH SER A  440  UNP  O88703              EXPRESSION TAG                 
SEQADV 5KHH ASN A  441  UNP  O88703              EXPRESSION TAG                 
SEQADV 5KHH ALA A  442  UNP  O88703              EXPRESSION TAG                 
SEQRES   1 A  204  SER ASN ALA ASP SER SER ARG ARG GLN TYR GLN GLU LYS          
SEQRES   2 A  204  TYR LYS GLN VAL GLU GLN TYR MET SER PHE HIS LYS LEU          
SEQRES   3 A  204  PRO ALA ASP PHE ARG GLN LYS ILE HIS ASP TYR TYR GLU          
SEQRES   4 A  204  HIS ARG TYR GLN GLY LYS MET PHE ASP GLU ASP SER ILE          
SEQRES   5 A  204  LEU GLY GLU LEU ASN GLY PRO LEU ARG GLU GLU ILE VAL          
SEQRES   6 A  204  ASN PHE ASN CSX ARG LYS LEU VAL ALA SER MET PRO LEU          
SEQRES   7 A  204  PHE ALA ASN ALA ASP PRO ASN PHE VAL THR ALA MET LEU          
SEQRES   8 A  204  THR LYS LEU LYS PHE GLU VAL PHE GLN PRO GLY ASP TYR          
SEQRES   9 A  204  ILE ILE ARG GLU GLY THR ILE GLY LYS LYS MET TYR PHE          
SEQRES  10 A  204  ILE GLN HIS GLY VAL VAL SER VAL LEU THR LYS GLY ASN          
SEQRES  11 A  204  LYS GLU MET LYS LEU SER ASP GLY SER TYR PHE GLY GLU          
SEQRES  12 A  204  ILE CYS LEU LEU THR ARG GLY ARG ARG THR ALA SER VAL          
SEQRES  13 A  204  ARG ALA ASP THR TYR CYS ARG LEU TYR SER LEU SER VAL          
SEQRES  14 A  204  ASP ASN PHE ASN GLU VAL LEU GLU GLU TYR PRO MET MET          
SEQRES  15 A  204  ARG ARG ALA PHE GLU THR VAL ALA ILE ASP ARG LEU ASP          
SEQRES  16 A  204  ARG ILE GLY LYS LYS ASN SER ILE LEU                          
MODRES 5KHH CSX A  508  CYS  MODIFIED RESIDUE                                   
HET    CSX  A 508       7                                                       
HET    6SW  A 701      22                                                       
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM     6SW INOSINE-3',5'-CYCLIC MONOPHOSPHATE                               
HETSYN     6SW CIMP                                                             
FORMUL   1  CSX    C3 H7 N O3 S                                                 
FORMUL   2  6SW    C10 H11 N4 O7 P                                              
FORMUL   3  HOH   *165(H2 O)                                                    
HELIX    1 AA1 SER A  444  HIS A  463  1                                  20    
HELIX    2 AA2 PRO A  466  GLN A  482  1                                  17    
HELIX    3 AA3 ASP A  487  LEU A  495  1                                   9    
HELIX    4 AA4 ASN A  496  CSX A  508  1                                  13    
HELIX    5 AA5 CSX A  508  SER A  514  1                                   7    
HELIX    6 AA6 MET A  515  ASN A  520  1                                   6    
HELIX    7 AA7 ASP A  522  THR A  531  1                                  10    
HELIX    8 AA8 GLY A  581  ARG A  588  1                                   8    
HELIX    9 AA9 VAL A  608  TYR A  618  1                                  11    
HELIX   10 AB1 PRO A  619  ILE A  636  1                                  18    
SHEET    1 AA1 4 LYS A 534  PHE A 538  0                                        
SHEET    2 AA1 4 CYS A 601  SER A 607 -1  O  LEU A 603   N  GLU A 536           
SHEET    3 AA1 4 LYS A 553  HIS A 559 -1  N  HIS A 559   O  ARG A 602           
SHEET    4 AA1 4 TYR A 579  PHE A 580 -1  O  PHE A 580   N  TYR A 555           
SHEET    1 AA2 4 TYR A 543  ILE A 545  0                                        
SHEET    2 AA2 4 SER A 594  ALA A 597 -1  O  VAL A 595   N  ILE A 545           
SHEET    3 AA2 4 VAL A 562  LEU A 565 -1  N  SER A 563   O  ARG A 596           
SHEET    4 AA2 4 MET A 572  LEU A 574 -1  O  MET A 572   N  VAL A 564           
LINK         C   ASN A 507                 N   CSX A 508     1555   1555  1.33  
LINK         C   CSX A 508                 N   ARG A 509     1555   1555  1.33  
SITE     1 AC1 12 MET A 572  PHE A 580  GLY A 581  GLU A 582                    
SITE     2 AC1 12 ILE A 583  CYS A 584  ARG A 591  THR A 592                    
SITE     3 AC1 12 ALA A 593  ARG A 632  ARG A 635  ILE A 636                    
CRYST1   96.037   96.037  115.913  90.00  90.00  90.00 I 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010413  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010413  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008627        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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