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Database: PDB
Entry: 3U0Z
LinkDB: 3U0Z
Original site: 3U0Z 
HEADER    TRANSPORT PROTEIN                       29-SEP-11   3U0Z              
TITLE     TETRAMERIZATION DYNAMICS OF THE C-TERMINUS UNDERLIES ISOFORM-SPECIFIC 
TITLE    2 CAMP-GATING IN HCN CHANNELS                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC        
COMPND   3 NUCLEOTIDE-GATED CHANNEL 1;                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 390-592);                  
COMPND   6 SYNONYM: BRAIN CYCLIC NUCLEOTIDE-GATED CHANNEL 1, BCNG-1,            
COMPND   7 HYPERPOLARIZATION-ACTIVATED CATION CHANNEL 2, HAC-2;                 
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: HCN1, BCNG1, HAC2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K12 ROSETTA CODON PLUS;                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET-24 WITH LIC CLONING CASSETTE 
KEYWDS    HELIX, BETA SHEET, TRANSPORT PROTEIN, CNMP BINDING                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LOLICATO,M.NARDINI,S.GAZZARRINI,S.MOLLER,D.BERTINETTI,F.W.HERBERG,  
AUTHOR   2 M.BOLOGNESI,H.MARTIN,M.FASOLINI,J.A.BERTRAND,C.ARRIGONI,G.THIEL,     
AUTHOR   3 A.MORONI                                                             
REVDAT   2   10-JUL-13 3U0Z    1       JRNL                                     
REVDAT   1   26-OCT-11 3U0Z    0                                                
JRNL        AUTH   M.LOLICATO,M.NARDINI,S.GAZZARRINI,S.MOLLER,D.BERTINETTI,     
JRNL        AUTH 2 F.W.HERBERG,M.BOLOGNESI,H.MARTIN,M.FASOLINI,J.A.BERTRAND,    
JRNL        AUTH 3 C.ARRIGONI,G.THIEL,A.MORONI                                  
JRNL        TITL   TETRAMERIZATION DYNAMICS OF C-TERMINAL DOMAIN UNDERLIES      
JRNL        TITL 2 ISOFORM-SPECIFIC CAMP GATING IN HYPERPOLARIZATION-ACTIVATED  
JRNL        TITL 3 CYCLIC NUCLEOTIDE-GATED CHANNELS.                            
JRNL        REF    J.BIOL.CHEM.                  V. 286 44811 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22006928                                                     
JRNL        DOI    10.1074/JBC.M111.297606                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 11258                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 560                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 828                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.4840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3278                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : 0.11000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.444         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.312         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.696        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.857                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3399 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4570 ; 1.708 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   397 ; 7.178 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   177 ;34.042 ;23.220       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   632 ;22.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;21.400 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   478 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2573 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1981 ; 0.658 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3195 ; 1.359 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1418 ; 2.004 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1374 ; 3.492 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    390       A     588      2                      
REMARK   3           1     B    390       B     588      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    794 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    836 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    794 ;  0.17 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    836 ;  0.22 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3U0Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068168.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97238                            
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 12.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.12000                            
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) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1Q43                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22% PEG 3350, 0.4M SODIUM ACETATE     
REMARK 280  BUFFER (PH 5.0), VAPOR DIFFUSION, TEMPERATURE 278K                  
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       48.83500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.83500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.60000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.83500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.83500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.60000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       48.83500            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       48.83500            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       56.60000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       48.83500            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       48.83500            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       56.60000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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      -97.67000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -97.67000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      -97.67000            
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      -97.67000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 11280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
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     GLN A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     PRO A   388                                                      
REMARK 465     MET A   389                                                      
REMARK 465     ILE A   589                                                      
REMARK 465     LEU A   590                                                      
REMARK 465     LEU A   591                                                      
REMARK 465     GLN A   592                                                      
REMARK 465     GLN B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     PRO B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     PRO B   388                                                      
REMARK 465     MET B   389                                                      
REMARK 465     ILE B   589                                                      
REMARK 465     LEU B   590                                                      
REMARK 465     LEU B   591                                                      
REMARK 465     GLN B   592                                                      
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 517     -160.39     61.71                                   
REMARK 500    LYS B 517     -163.31     61.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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: 1Q43   RELATED DB: PDB                                   
REMARK 900 HCN2I 443-640 IN THE PRESENCE OF CAMP, SELENOMETHIONINE              
REMARK 900 DERIVATIVE                                                           
REMARK 900 RELATED ID: 3OTF   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR THE CAMP-DEPENDENT GATING IN HUMAN              
REMARK 900 HCN4 CHANNEL                                                         
REMARK 900 RELATED ID: 3U10   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U11   RELATED DB: PDB                                   
DBREF  3U0Z A  390   592  UNP    O88704   HCN1_MOUSE     390    592             
DBREF  3U0Z B  390   592  UNP    O88704   HCN1_MOUSE     390    592             
SEQADV 3U0Z GLN A  383  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z GLY A  384  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z PRO A  385  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z SER A  386  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z SER A  387  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z PRO A  388  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z MET A  389  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z GLN B  383  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z GLY B  384  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z PRO B  385  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z SER B  386  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z SER B  387  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z PRO B  388  UNP  O88704              EXPRESSION TAG                 
SEQADV 3U0Z MET B  389  UNP  O88704              EXPRESSION TAG                 
SEQRES   1 A  210  GLN GLY PRO SER SER PRO MET ASP SER SER ARG ARG GLN          
SEQRES   2 A  210  TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN TYR MET SER          
SEQRES   3 A  210  PHE HIS LYS LEU PRO ALA ASP MET ARG GLN LYS ILE HIS          
SEQRES   4 A  210  ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS ILE PHE ASP          
SEQRES   5 A  210  GLU GLU ASN ILE LEU SER GLU LEU ASN ASP PRO LEU ARG          
SEQRES   6 A  210  GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS LEU VAL ALA          
SEQRES   7 A  210  THR MET PRO LEU PHE ALA ASN ALA ASP PRO ASN PHE VAL          
SEQRES   8 A  210  THR ALA MET LEU SER LYS LEU ARG PHE GLU VAL PHE GLN          
SEQRES   9 A  210  PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA VAL GLY LYS          
SEQRES  10 A  210  LYS MET TYR PHE ILE GLN HIS GLY VAL ALA GLY VAL ILE          
SEQRES  11 A  210  THR LYS SER SER LYS GLU MET LYS LEU THR ASP GLY SER          
SEQRES  12 A  210  TYR PHE GLY GLU ILE CYS LEU LEU THR LYS GLY ARG ARG          
SEQRES  13 A  210  THR ALA SER VAL ARG ALA ASP THR TYR CYS ARG LEU TYR          
SEQRES  14 A  210  SER LEU SER VAL ASP ASN PHE ASN GLU VAL LEU GLU GLU          
SEQRES  15 A  210  TYR PRO MET MET ARG ARG ALA PHE GLU THR VAL ALA ILE          
SEQRES  16 A  210  ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN SER ILE LEU          
SEQRES  17 A  210  LEU GLN                                                      
SEQRES   1 B  210  GLN GLY PRO SER SER PRO MET ASP SER SER ARG ARG GLN          
SEQRES   2 B  210  TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN TYR MET SER          
SEQRES   3 B  210  PHE HIS LYS LEU PRO ALA ASP MET ARG GLN LYS ILE HIS          
SEQRES   4 B  210  ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS ILE PHE ASP          
SEQRES   5 B  210  GLU GLU ASN ILE LEU SER GLU LEU ASN ASP PRO LEU ARG          
SEQRES   6 B  210  GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS LEU VAL ALA          
SEQRES   7 B  210  THR MET PRO LEU PHE ALA ASN ALA ASP PRO ASN PHE VAL          
SEQRES   8 B  210  THR ALA MET LEU SER LYS LEU ARG PHE GLU VAL PHE GLN          
SEQRES   9 B  210  PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA VAL GLY LYS          
SEQRES  10 B  210  LYS MET TYR PHE ILE GLN HIS GLY VAL ALA GLY VAL ILE          
SEQRES  11 B  210  THR LYS SER SER LYS GLU MET LYS LEU THR ASP GLY SER          
SEQRES  12 B  210  TYR PHE GLY GLU ILE CYS LEU LEU THR LYS GLY ARG ARG          
SEQRES  13 B  210  THR ALA SER VAL ARG ALA ASP THR TYR CYS ARG LEU TYR          
SEQRES  14 B  210  SER LEU SER VAL ASP ASN PHE ASN GLU VAL LEU GLU GLU          
SEQRES  15 B  210  TYR PRO MET MET ARG ARG ALA PHE GLU THR VAL ALA ILE          
SEQRES  16 B  210  ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN SER ILE LEU          
SEQRES  17 B  210  LEU GLN                                                      
HET    CMP  A 646      22                                                       
HET    CMP  B 646      22                                                       
HETNAM     CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE                             
HETSYN     CMP CYCLIC AMP; CAMP                                                 
FORMUL   3  CMP    2(C10 H12 N5 O6 P)                                           
FORMUL   5  HOH   *49(H2 O)                                                     
HELIX    1   1 ASP A  390  LYS A  411  1                                  22    
HELIX    2   2 PRO A  413  GLN A  429  1                                  17    
HELIX    3   3 ASP A  434  GLU A  441  1                                   8    
HELIX    4   4 ASN A  443  CYS A  455  1                                  13    
HELIX    5   5 CYS A  455  THR A  461  1                                   7    
HELIX    6   6 MET A  462  ASN A  467  1                                   6    
HELIX    7   7 ASP A  469  LYS A  479  1                                  11    
HELIX    8   8 GLY A  528  LYS A  535  1                                   8    
HELIX    9   9 VAL A  555  TYR A  565  1                                  11    
HELIX   10  10 PRO A  566  GLY A  584  1                                  19    
HELIX   11  11 SER B  391  LYS B  411  1                                  21    
HELIX   12  12 PRO B  413  GLN B  429  1                                  17    
HELIX   13  13 ASP B  434  GLU B  441  1                                   8    
HELIX   14  14 ASN B  443  CYS B  455  1                                  13    
HELIX   15  15 CYS B  455  THR B  461  1                                   7    
HELIX   16  16 MET B  462  ASN B  467  1                                   6    
HELIX   17  17 ASP B  469  LEU B  480  1                                  12    
HELIX   18  18 GLY B  528  LYS B  535  1                                   8    
HELIX   19  19 VAL B  555  TYR B  565  1                                  11    
HELIX   20  20 PRO B  566  ILE B  583  1                                  18    
SHEET    1   A 4 ARG A 481  PHE A 485  0                                        
SHEET    2   A 4 CYS A 548  SER A 554 -1  O  SER A 552   N  ARG A 481           
SHEET    3   A 4 LYS A 500  HIS A 506 -1  N  HIS A 506   O  ARG A 549           
SHEET    4   A 4 TYR A 526  PHE A 527 -1  O  PHE A 527   N  TYR A 502           
SHEET    1   B 4 TYR A 490  ILE A 492  0                                        
SHEET    2   B 4 SER A 541  ALA A 544 -1  O  VAL A 542   N  ILE A 492           
SHEET    3   B 4 ALA A 509  ILE A 512 -1  N  ILE A 512   O  SER A 541           
SHEET    4   B 4 MET A 519  LEU A 521 -1  O  LEU A 521   N  ALA A 509           
SHEET    1   C 4 ARG B 481  PHE B 485  0                                        
SHEET    2   C 4 CYS B 548  SER B 554 -1  O  SER B 552   N  ARG B 481           
SHEET    3   C 4 LYS B 500  HIS B 506 -1  N  HIS B 506   O  ARG B 549           
SHEET    4   C 4 TYR B 526  PHE B 527 -1  O  PHE B 527   N  TYR B 502           
SHEET    1   D 4 TYR B 490  ILE B 492  0                                        
SHEET    2   D 4 SER B 541  ALA B 544 -1  O  VAL B 542   N  ILE B 492           
SHEET    3   D 4 ALA B 509  ILE B 512 -1  N  ILE B 512   O  SER B 541           
SHEET    4   D 4 MET B 519  LEU B 521 -1  O  LEU B 521   N  ALA B 509           
SITE     1 AC1 11 VAL A 511  PHE A 527  GLY A 528  GLU A 529                    
SITE     2 AC1 11 ILE A 530  CYS A 531  ARG A 538  THR A 539                    
SITE     3 AC1 11 ALA A 540  ARG A 579  ARG A 582                               
SITE     1 AC2 11 VAL B 511  PHE B 527  GLY B 528  GLU B 529                    
SITE     2 AC2 11 ILE B 530  CYS B 531  ARG B 538  THR B 539                    
SITE     3 AC2 11 ALA B 540  ARG B 579  ARG B 582                               
CRYST1   97.670   97.670  113.200  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      0.010239  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010239  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008834        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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