GenomeNet

Database: PDB
Entry: 6GYN
LinkDB: 6GYN
Original site: 6GYN 
HEADER    MEMBRANE PROTEIN                        30-JUN-18   6GYN              
TITLE     STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-
TITLE    2 GATED ION CHANNEL                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC        
COMPND   3 NUCLEOTIDE-GATED CHANNEL 4;                                          
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCN4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE                               
KEYWDS    ION CHANNEL, PACEMAKER CURRENT, STRUCTURAL GENOMICS, STRUCTURAL       
KEYWDS   2 GENOMICS CONSORTIUM, SGC, MEMBRANE PROTEIN                           
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    C.A.SHINTRE,A.C.W.PIKE,A.TESSITORE,M.YOUNG,S.R.BUSHELL,C.STRAIN-      
AUTHOR   2 DAMERELL,S.MUKHOPADHYAY,N.A.BURGESS-BROWN,J.T.HUISKONEN,             
AUTHOR   3 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,E.P.CARPENTER,STRUCTURAL        
AUTHOR   4 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   2   11-DEC-19 6GYN    1       SCALE                                    
REVDAT   1   08-MAY-19 6GYN    0                                                
JRNL        AUTH   C.A.SHINTRE,A.C.W.PIKE,A.TESSITORE,M.YOUNG,S.R.BUSHELL,      
JRNL        AUTH 2 C.STRAIN-DAMERELL,S.MUKHOPADHYAY,N.A.BURGESS-BROWN,          
JRNL        AUTH 3 J.T.HUISKONEN,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,          
JRNL        AUTH 4 E.P.CARPENTER                                                
JRNL        TITL   STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC   
JRNL        TITL 2 NUCLEOTIDE-GATED ION CHANNEL                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : GAUTOMATCH, EPU, CTFFIND, COOT, PHENIX,   
REMARK   3                            RELION, RELION, RELION, CRYOSPARC         
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : AB INITIO MODEL                     
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : MODEL REFINED AGAINST THE CRYOSPARC B-FACTOR     
REMARK   3  SHARPENED MAP USING DEFAULT RESTRAINTS                              
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.400                          
REMARK   3   NUMBER OF PARTICLES               : 25764                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6GYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010747.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : POTASSIUM/SODIUM                  
REMARK 245                                    HYPERPOLARIZATION-ACTIVATED       
REMARK 245                                    CYCLIC NUCLEOTIDE-GATED ION       
REMARK 245                                    CHANNEL 4                         
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 5.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOTTED FOR 5.5S BEFORE PLUNGE    
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 1294                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1300.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 48.70                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 37313                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : EBIC TITAN KRIOS M02           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: 54070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 87250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -416.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   199                                                      
REMARK 465     MET A   200                                                      
REMARK 465     LEU A   201                                                      
REMARK 465     PRO A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     GLU A   205                                                      
REMARK 465     VAL A   206                                                      
REMARK 465     ARG A   207                                                      
REMARK 465     LEU A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     GLN A   210                                                      
REMARK 465     ALA A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     PHE A   213                                                      
REMARK 465     ASP A   709                                                      
REMARK 465     ARG A   710                                                      
REMARK 465     LEU A   711                                                      
REMARK 465     ASP A   712                                                      
REMARK 465     ARG A   713                                                      
REMARK 465     ILE A   714                                                      
REMARK 465     GLY A   715                                                      
REMARK 465     LYS A   716                                                      
REMARK 465     LYS A   717                                                      
REMARK 465     ASN A   718                                                      
REMARK 465     SER A   719                                                      
REMARK 465     SER B   199                                                      
REMARK 465     MET B   200                                                      
REMARK 465     LEU B   201                                                      
REMARK 465     PRO B   202                                                      
REMARK 465     GLU B   203                                                      
REMARK 465     ALA B   204                                                      
REMARK 465     GLU B   205                                                      
REMARK 465     VAL B   206                                                      
REMARK 465     ARG B   207                                                      
REMARK 465     LEU B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     GLN B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     PHE B   213                                                      
REMARK 465     ASP B   709                                                      
REMARK 465     ARG B   710                                                      
REMARK 465     LEU B   711                                                      
REMARK 465     ASP B   712                                                      
REMARK 465     ARG B   713                                                      
REMARK 465     ILE B   714                                                      
REMARK 465     GLY B   715                                                      
REMARK 465     LYS B   716                                                      
REMARK 465     LYS B   717                                                      
REMARK 465     ASN B   718                                                      
REMARK 465     SER B   719                                                      
REMARK 465     SER C   199                                                      
REMARK 465     MET C   200                                                      
REMARK 465     LEU C   201                                                      
REMARK 465     PRO C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     ALA C   204                                                      
REMARK 465     GLU C   205                                                      
REMARK 465     VAL C   206                                                      
REMARK 465     ARG C   207                                                      
REMARK 465     LEU C   208                                                      
REMARK 465     GLY C   209                                                      
REMARK 465     GLN C   210                                                      
REMARK 465     ALA C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     PHE C   213                                                      
REMARK 465     ASP C   709                                                      
REMARK 465     ARG C   710                                                      
REMARK 465     LEU C   711                                                      
REMARK 465     ASP C   712                                                      
REMARK 465     ARG C   713                                                      
REMARK 465     ILE C   714                                                      
REMARK 465     GLY C   715                                                      
REMARK 465     LYS C   716                                                      
REMARK 465     LYS C   717                                                      
REMARK 465     ASN C   718                                                      
REMARK 465     SER C   719                                                      
REMARK 465     SER D   199                                                      
REMARK 465     MET D   200                                                      
REMARK 465     LEU D   201                                                      
REMARK 465     PRO D   202                                                      
REMARK 465     GLU D   203                                                      
REMARK 465     ALA D   204                                                      
REMARK 465     GLU D   205                                                      
REMARK 465     VAL D   206                                                      
REMARK 465     ARG D   207                                                      
REMARK 465     LEU D   208                                                      
REMARK 465     GLY D   209                                                      
REMARK 465     GLN D   210                                                      
REMARK 465     ALA D   211                                                      
REMARK 465     GLY D   212                                                      
REMARK 465     PHE D   213                                                      
REMARK 465     ASP D   709                                                      
REMARK 465     ARG D   710                                                      
REMARK 465     LEU D   711                                                      
REMARK 465     ASP D   712                                                      
REMARK 465     ARG D   713                                                      
REMARK 465     ILE D   714                                                      
REMARK 465     GLY D   715                                                      
REMARK 465     LYS D   716                                                      
REMARK 465     LYS D   717                                                      
REMARK 465     ASN D   718                                                      
REMARK 465     SER D   719                                                      
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     ARG A 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 291    CG   OD1  ND2                                       
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 322    CG   OD1  OD2                                       
REMARK 470     ASN A 323    CG   OD1  ND2                                       
REMARK 470     THR A 324    OG1  CG2                                            
REMARK 470     GLU A 325    CD   OE1  OE2                                       
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     GLU A 403    CD   OE1  OE2                                       
REMARK 470     GLN A 484    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 567    CD   OE1  OE2                                       
REMARK 470     ASN A 598    CG   OD1  ND2                                       
REMARK 470     LYS A 630    CD   CE   NZ                                        
REMARK 470     ASN A 647    CG   OD1  ND2                                       
REMARK 470     ARG A 666    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 708    CG   CD1  CD2                                       
REMARK 470     ARG B 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 290    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 291    CG   OD1  ND2                                       
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 322    CG   OD1  OD2                                       
REMARK 470     ASN B 323    CG   OD1  ND2                                       
REMARK 470     THR B 324    OG1  CG2                                            
REMARK 470     GLU B 325    CD   OE1  OE2                                       
REMARK 470     LYS B 369    CG   CD   CE   NZ                                   
REMARK 470     GLU B 403    CD   OE1  OE2                                       
REMARK 470     GLN B 484    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 567    CD   OE1  OE2                                       
REMARK 470     ASN B 598    CG   OD1  ND2                                       
REMARK 470     LYS B 630    CD   CE   NZ                                        
REMARK 470     ASN B 647    CG   OD1  ND2                                       
REMARK 470     ARG B 666    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 708    CG   CD1  CD2                                       
REMARK 470     ARG C 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 290    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 291    CG   OD1  ND2                                       
REMARK 470     GLU C 321    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 322    CG   OD1  OD2                                       
REMARK 470     ASN C 323    CG   OD1  ND2                                       
REMARK 470     THR C 324    OG1  CG2                                            
REMARK 470     GLU C 325    CD   OE1  OE2                                       
REMARK 470     LYS C 369    CG   CD   CE   NZ                                   
REMARK 470     GLU C 403    CD   OE1  OE2                                       
REMARK 470     GLN C 484    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 567    CD   OE1  OE2                                       
REMARK 470     ASN C 598    CG   OD1  ND2                                       
REMARK 470     LYS C 630    CD   CE   NZ                                        
REMARK 470     ASN C 647    CG   OD1  ND2                                       
REMARK 470     ARG C 666    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 708    CG   CD1  CD2                                       
REMARK 470     ARG D 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE D 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D 290    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 291    CG   OD1  ND2                                       
REMARK 470     GLU D 321    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 322    CG   OD1  OD2                                       
REMARK 470     ASN D 323    CG   OD1  ND2                                       
REMARK 470     THR D 324    OG1  CG2                                            
REMARK 470     GLU D 325    CD   OE1  OE2                                       
REMARK 470     LYS D 369    CG   CD   CE   NZ                                   
REMARK 470     GLU D 403    CD   OE1  OE2                                       
REMARK 470     GLN D 484    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 567    CD   OE1  OE2                                       
REMARK 470     ASN D 598    CG   OD1  ND2                                       
REMARK 470     LYS D 630    CD   CE   NZ                                        
REMARK 470     ASN D 647    CG   OD1  ND2                                       
REMARK 470     ARG D 666    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 708    CG   CD1  CD2                                       
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    TRP A 253       63.64     60.64                                   
REMARK 500    GLU A 290       31.91    -94.42                                   
REMARK 500    TRP A 341       30.72   -140.86                                   
REMARK 500    PHE A 445       74.59     53.10                                   
REMARK 500    TYR A 481     -154.34    -94.89                                   
REMARK 500    TRP B 253       63.52     60.72                                   
REMARK 500    GLU B 290       31.86    -94.38                                   
REMARK 500    TRP B 341       30.72   -140.82                                   
REMARK 500    PHE B 445       74.62     53.04                                   
REMARK 500    TYR B 481     -154.31    -94.98                                   
REMARK 500    TRP C 253       63.63     60.67                                   
REMARK 500    GLU C 290       32.00    -94.43                                   
REMARK 500    TRP C 341       30.69   -140.80                                   
REMARK 500    PHE C 445       74.55     53.12                                   
REMARK 500    TYR C 481     -154.35    -94.92                                   
REMARK 500    TRP D 253       63.63     60.67                                   
REMARK 500    GLU D 290       32.00    -94.43                                   
REMARK 500    TRP D 341       30.69   -140.80                                   
REMARK 500    PHE D 445       74.62     53.01                                   
REMARK 500    TYR D 481     -154.35    -94.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PC1 A  801                                                       
REMARK 610     PC1 A  802                                                       
REMARK 610     PC1 A  803                                                       
REMARK 610     3PE A  804                                                       
REMARK 610     3PE A  805                                                       
REMARK 610     PC1 A  806                                                       
REMARK 610     PC1 A  807                                                       
REMARK 610     PC1 A  808                                                       
REMARK 610     PC1 A  809                                                       
REMARK 610     PC1 B  801                                                       
REMARK 610     PC1 B  802                                                       
REMARK 610     PC1 B  803                                                       
REMARK 610     PC1 B  804                                                       
REMARK 610     PC1 B  805                                                       
REMARK 610     3PE B  806                                                       
REMARK 610     3PE B  807                                                       
REMARK 610     PC1 B  808                                                       
REMARK 610     PC1 B  809                                                       
REMARK 610     PC1 C  801                                                       
REMARK 610     PC1 C  802                                                       
REMARK 610     PC1 C  803                                                       
REMARK 610     PC1 C  804                                                       
REMARK 610     PC1 C  805                                                       
REMARK 610     3PE C  806                                                       
REMARK 610     3PE C  807                                                       
REMARK 610     PC1 C  808                                                       
REMARK 610     PC1 C  809                                                       
REMARK 610     PC1 D  801                                                       
REMARK 610     PC1 D  802                                                       
REMARK 610     PC1 D  803                                                       
REMARK 610     PC1 D  804                                                       
REMARK 610     PC1 D  805                                                       
REMARK 610     PC1 D  806                                                       
REMARK 610     PC1 D  807                                                       
REMARK 610     3PE D  808                                                       
REMARK 610     3PE D  809                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-0093   RELATED DB: EMDB                              
REMARK 900 STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC           
REMARK 900 NUCLEOTIDE-GATED ION CHANNEL                                         
DBREF  6GYN A  201   719  UNP    Q9Y3Q4   HCN4_HUMAN     201    719             
DBREF  6GYN B  201   719  UNP    Q9Y3Q4   HCN4_HUMAN     201    719             
DBREF  6GYN C  201   719  UNP    Q9Y3Q4   HCN4_HUMAN     201    719             
DBREF  6GYN D  201   719  UNP    Q9Y3Q4   HCN4_HUMAN     201    719             
SEQADV 6GYN SER A  199  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN MET A  200  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN SER B  199  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN MET B  200  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN SER C  199  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN MET C  200  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN SER D  199  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQADV 6GYN MET D  200  UNP  Q9Y3Q4              EXPRESSION TAG                 
SEQRES   1 A  521  SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA          
SEQRES   2 A  521  GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO          
SEQRES   3 A  521  GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN          
SEQRES   4 A  521  LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA          
SEQRES   5 A  521  GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE          
SEQRES   6 A  521  TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN          
SEQRES   7 A  521  LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP          
SEQRES   8 A  521  GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER          
SEQRES   9 A  521  ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG          
SEQRES  10 A  521  THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU          
SEQRES  11 A  521  ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP          
SEQRES  12 A  521  PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR          
SEQRES  13 A  521  ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL          
SEQRES  14 A  521  TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR          
SEQRES  15 A  521  LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG          
SEQRES  16 A  521  LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS          
SEQRES  17 A  521  MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL          
SEQRES  18 A  521  ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP          
SEQRES  19 A  521  GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE          
SEQRES  20 A  521  PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN          
SEQRES  21 A  521  ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS          
SEQRES  22 A  521  ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN          
SEQRES  23 A  521  ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU          
SEQRES  24 A  521  SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE          
SEQRES  25 A  521  GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER          
SEQRES  26 A  521  ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN          
SEQRES  27 A  521  TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN          
SEQRES  28 A  521  ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS          
SEQRES  29 A  521  MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU          
SEQRES  30 A  521  PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS          
SEQRES  31 A  521  LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO          
SEQRES  32 A  521  ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU          
SEQRES  33 A  521  VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR          
SEQRES  34 A  521  ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL          
SEQRES  35 A  521  SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA          
SEQRES  36 A  521  ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG          
SEQRES  37 A  521  GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS          
SEQRES  38 A  521  ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL          
SEQRES  39 A  521  LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR          
SEQRES  40 A  521  VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN          
SEQRES  41 A  521  SER                                                          
SEQRES   1 B  521  SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA          
SEQRES   2 B  521  GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO          
SEQRES   3 B  521  GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN          
SEQRES   4 B  521  LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA          
SEQRES   5 B  521  GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE          
SEQRES   6 B  521  TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN          
SEQRES   7 B  521  LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP          
SEQRES   8 B  521  GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER          
SEQRES   9 B  521  ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG          
SEQRES  10 B  521  THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU          
SEQRES  11 B  521  ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP          
SEQRES  12 B  521  PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR          
SEQRES  13 B  521  ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL          
SEQRES  14 B  521  TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR          
SEQRES  15 B  521  LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG          
SEQRES  16 B  521  LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS          
SEQRES  17 B  521  MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL          
SEQRES  18 B  521  ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP          
SEQRES  19 B  521  GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE          
SEQRES  20 B  521  PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN          
SEQRES  21 B  521  ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS          
SEQRES  22 B  521  ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN          
SEQRES  23 B  521  ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU          
SEQRES  24 B  521  SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE          
SEQRES  25 B  521  GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER          
SEQRES  26 B  521  ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN          
SEQRES  27 B  521  TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN          
SEQRES  28 B  521  ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS          
SEQRES  29 B  521  MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU          
SEQRES  30 B  521  PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS          
SEQRES  31 B  521  LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO          
SEQRES  32 B  521  ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU          
SEQRES  33 B  521  VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR          
SEQRES  34 B  521  ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL          
SEQRES  35 B  521  SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA          
SEQRES  36 B  521  ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG          
SEQRES  37 B  521  GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS          
SEQRES  38 B  521  ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL          
SEQRES  39 B  521  LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR          
SEQRES  40 B  521  VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN          
SEQRES  41 B  521  SER                                                          
SEQRES   1 C  521  SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA          
SEQRES   2 C  521  GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO          
SEQRES   3 C  521  GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN          
SEQRES   4 C  521  LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA          
SEQRES   5 C  521  GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE          
SEQRES   6 C  521  TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN          
SEQRES   7 C  521  LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP          
SEQRES   8 C  521  GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER          
SEQRES   9 C  521  ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG          
SEQRES  10 C  521  THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU          
SEQRES  11 C  521  ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP          
SEQRES  12 C  521  PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR          
SEQRES  13 C  521  ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL          
SEQRES  14 C  521  TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR          
SEQRES  15 C  521  LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG          
SEQRES  16 C  521  LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS          
SEQRES  17 C  521  MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL          
SEQRES  18 C  521  ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP          
SEQRES  19 C  521  GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE          
SEQRES  20 C  521  PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN          
SEQRES  21 C  521  ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS          
SEQRES  22 C  521  ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN          
SEQRES  23 C  521  ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU          
SEQRES  24 C  521  SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE          
SEQRES  25 C  521  GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER          
SEQRES  26 C  521  ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN          
SEQRES  27 C  521  TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN          
SEQRES  28 C  521  ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS          
SEQRES  29 C  521  MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU          
SEQRES  30 C  521  PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS          
SEQRES  31 C  521  LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO          
SEQRES  32 C  521  ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU          
SEQRES  33 C  521  VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR          
SEQRES  34 C  521  ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL          
SEQRES  35 C  521  SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA          
SEQRES  36 C  521  ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG          
SEQRES  37 C  521  GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS          
SEQRES  38 C  521  ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL          
SEQRES  39 C  521  LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR          
SEQRES  40 C  521  VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN          
SEQRES  41 C  521  SER                                                          
SEQRES   1 D  521  SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA          
SEQRES   2 D  521  GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO          
SEQRES   3 D  521  GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN          
SEQRES   4 D  521  LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA          
SEQRES   5 D  521  GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE          
SEQRES   6 D  521  TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN          
SEQRES   7 D  521  LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP          
SEQRES   8 D  521  GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER          
SEQRES   9 D  521  ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG          
SEQRES  10 D  521  THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU          
SEQRES  11 D  521  ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP          
SEQRES  12 D  521  PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR          
SEQRES  13 D  521  ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL          
SEQRES  14 D  521  TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR          
SEQRES  15 D  521  LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG          
SEQRES  16 D  521  LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS          
SEQRES  17 D  521  MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL          
SEQRES  18 D  521  ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP          
SEQRES  19 D  521  GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE          
SEQRES  20 D  521  PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN          
SEQRES  21 D  521  ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS          
SEQRES  22 D  521  ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN          
SEQRES  23 D  521  ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU          
SEQRES  24 D  521  SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE          
SEQRES  25 D  521  GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER          
SEQRES  26 D  521  ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN          
SEQRES  27 D  521  TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN          
SEQRES  28 D  521  ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS          
SEQRES  29 D  521  MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU          
SEQRES  30 D  521  PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS          
SEQRES  31 D  521  LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO          
SEQRES  32 D  521  ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU          
SEQRES  33 D  521  VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR          
SEQRES  34 D  521  ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL          
SEQRES  35 D  521  SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA          
SEQRES  36 D  521  ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG          
SEQRES  37 D  521  GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS          
SEQRES  38 D  521  ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL          
SEQRES  39 D  521  LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR          
SEQRES  40 D  521  VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN          
SEQRES  41 D  521  SER                                                          
HET    PC1  A 801      36                                                       
HET    PC1  A 802      29                                                       
HET    PC1  A 803      14                                                       
HET    3PE  A 804      30                                                       
HET    3PE  A 805      32                                                       
HET    PC1  A 806      23                                                       
HET    PC1  A 807      15                                                       
HET    PC1  A 808      35                                                       
HET    PC1  A 809      15                                                       
HET    PC1  B 801      35                                                       
HET    PC1  B 802      15                                                       
HET    PC1  B 803      36                                                       
HET    PC1  B 804      29                                                       
HET    PC1  B 805      14                                                       
HET    3PE  B 806      30                                                       
HET    3PE  B 807      32                                                       
HET    PC1  B 808      23                                                       
HET    PC1  B 809      15                                                       
HET    PC1  C 801      35                                                       
HET    PC1  C 802      15                                                       
HET    PC1  C 803      36                                                       
HET    PC1  C 804      29                                                       
HET    PC1  C 805      14                                                       
HET    3PE  C 806      30                                                       
HET    3PE  C 807      32                                                       
HET    PC1  C 808      23                                                       
HET    PC1  C 809      15                                                       
HET    PC1  D 801      23                                                       
HET    PC1  D 802      15                                                       
HET    PC1  D 803      35                                                       
HET    PC1  D 804      15                                                       
HET    PC1  D 805      36                                                       
HET    PC1  D 806      29                                                       
HET    PC1  D 807      14                                                       
HET    3PE  D 808      30                                                       
HET    3PE  D 809      32                                                       
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETNAM     3PE 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE                      
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
HETSYN     3PE 3-SN-PHOSPHATIDYLETHANOLAMINE                                    
FORMUL   5  PC1    28(C44 H88 N O8 P)                                           
FORMUL   8  3PE    8(C41 H82 N O8 P)                                            
HELIX    1 AA1 ARG A  216  LEU A  222  1                                   7    
HELIX    2 AA2 ASN A  227  PHE A  234  1                                   8    
HELIX    3 AA3 SER A  236  SER A  249  1                                  14    
HELIX    4 AA4 SER A  259  PHE A  286  1                                  28    
HELIX    5 AA5 THR A  292  ASN A  313  1                                  22    
HELIX    6 AA6 PHE A  314  THR A  316  5                                   3    
HELIX    7 AA7 ASP A  329  TRP A  341  1                                  13    
HELIX    8 AA8 TRP A  341  ILE A  350  1                                  10    
HELIX    9 AA9 PRO A  351  ASP A  364  1                                  14    
HELIX   10 AB1 ALA A  371  SER A  384  1                                  14    
HELIX   11 AB2 LEU A  385  LEU A  389  5                                   5    
HELIX   12 AB3 ARG A  390  ASP A  410  1                                  21    
HELIX   13 AB4 ALA A  412  GLN A  443  1                                  32    
HELIX   14 AB5 CYS A  449  ASN A  454  1                                   6    
HELIX   15 AB6 SER A  460  HIS A  475  1                                  16    
HELIX   16 AB7 GLY A  488  GLN A  518  1                                  31    
HELIX   17 AB8 ASP A  521  HIS A  541  1                                  21    
HELIX   18 AB9 PRO A  544  TYR A  559  1                                  16    
HELIX   19 AC1 ASP A  565  LEU A  573  1                                   9    
HELIX   20 AC2 SER A  574  ALA A  591  1                                  18    
HELIX   21 AC3 ASP A  600  LEU A  608  1                                   9    
HELIX   22 AC4 THR A  609  LEU A  611  5                                   3    
HELIX   23 AC5 GLU A  660  ARG A  666  1                                   7    
HELIX   24 AC6 VAL A  686  TYR A  696  1                                  11    
HELIX   25 AC7 TYR A  696  LEU A  708  1                                  13    
HELIX   26 AC8 ARG B  216  LEU B  222  1                                   7    
HELIX   27 AC9 ASN B  227  PHE B  234  1                                   8    
HELIX   28 AD1 SER B  236  SER B  249  1                                  14    
HELIX   29 AD2 SER B  259  PHE B  286  1                                  28    
HELIX   30 AD3 THR B  292  ASN B  313  1                                  22    
HELIX   31 AD4 PHE B  314  THR B  316  5                                   3    
HELIX   32 AD5 ASP B  329  TRP B  341  1                                  13    
HELIX   33 AD6 TRP B  341  ILE B  350  1                                  10    
HELIX   34 AD7 PRO B  351  ASP B  364  1                                  14    
HELIX   35 AD8 ALA B  371  SER B  384  1                                  14    
HELIX   36 AD9 LEU B  385  LEU B  389  5                                   5    
HELIX   37 AE1 ARG B  390  ASP B  410  1                                  21    
HELIX   38 AE2 ALA B  412  GLN B  443  1                                  32    
HELIX   39 AE3 CYS B  449  ASN B  454  1                                   6    
HELIX   40 AE4 SER B  460  HIS B  475  1                                  16    
HELIX   41 AE5 GLY B  488  GLN B  518  1                                  31    
HELIX   42 AE6 ASP B  521  HIS B  541  1                                  21    
HELIX   43 AE7 PRO B  544  TYR B  559  1                                  16    
HELIX   44 AE8 ASP B  565  LEU B  573  1                                   9    
HELIX   45 AE9 SER B  574  ALA B  591  1                                  18    
HELIX   46 AF1 ASP B  600  LEU B  608  1                                   9    
HELIX   47 AF2 THR B  609  LEU B  611  5                                   3    
HELIX   48 AF3 GLU B  660  ARG B  666  1                                   7    
HELIX   49 AF4 VAL B  686  TYR B  696  1                                  11    
HELIX   50 AF5 TYR B  696  LEU B  708  1                                  13    
HELIX   51 AF6 ARG C  216  LEU C  222  1                                   7    
HELIX   52 AF7 ASN C  227  PHE C  234  1                                   8    
HELIX   53 AF8 SER C  236  SER C  249  1                                  14    
HELIX   54 AF9 SER C  259  PHE C  286  1                                  28    
HELIX   55 AG1 THR C  292  ASN C  313  1                                  22    
HELIX   56 AG2 PHE C  314  THR C  316  5                                   3    
HELIX   57 AG3 ASP C  329  TRP C  341  1                                  13    
HELIX   58 AG4 TRP C  341  ILE C  350  1                                  10    
HELIX   59 AG5 PRO C  351  ASP C  364  1                                  14    
HELIX   60 AG6 ALA C  371  SER C  384  1                                  14    
HELIX   61 AG7 LEU C  385  LEU C  389  5                                   5    
HELIX   62 AG8 ARG C  390  ASP C  410  1                                  21    
HELIX   63 AG9 ALA C  412  GLN C  443  1                                  32    
HELIX   64 AH1 CYS C  449  ASN C  454  1                                   6    
HELIX   65 AH2 SER C  460  HIS C  475  1                                  16    
HELIX   66 AH3 GLY C  488  GLN C  518  1                                  31    
HELIX   67 AH4 ASP C  521  HIS C  541  1                                  21    
HELIX   68 AH5 PRO C  544  TYR C  559  1                                  16    
HELIX   69 AH6 ASP C  565  LEU C  573  1                                   9    
HELIX   70 AH7 SER C  574  ALA C  591  1                                  18    
HELIX   71 AH8 ASP C  600  LEU C  608  1                                   9    
HELIX   72 AH9 THR C  609  LEU C  611  5                                   3    
HELIX   73 AI1 GLU C  660  ARG C  666  1                                   7    
HELIX   74 AI2 VAL C  686  TYR C  696  1                                  11    
HELIX   75 AI3 TYR C  696  LEU C  708  1                                  13    
HELIX   76 AI4 ARG D  216  LEU D  222  1                                   7    
HELIX   77 AI5 ASN D  227  PHE D  234  1                                   8    
HELIX   78 AI6 SER D  236  SER D  249  1                                  14    
HELIX   79 AI7 SER D  259  PHE D  286  1                                  28    
HELIX   80 AI8 THR D  292  ASN D  313  1                                  22    
HELIX   81 AI9 PHE D  314  THR D  316  5                                   3    
HELIX   82 AJ1 ASP D  329  TRP D  341  1                                  13    
HELIX   83 AJ2 TRP D  341  ILE D  350  1                                  10    
HELIX   84 AJ3 PRO D  351  ASP D  364  1                                  14    
HELIX   85 AJ4 ALA D  371  SER D  384  1                                  14    
HELIX   86 AJ5 LEU D  385  LEU D  389  5                                   5    
HELIX   87 AJ6 ARG D  390  ASP D  410  1                                  21    
HELIX   88 AJ7 ALA D  412  GLN D  443  1                                  32    
HELIX   89 AJ8 CYS D  449  ASN D  454  1                                   6    
HELIX   90 AJ9 SER D  460  HIS D  475  1                                  16    
HELIX   91 AK1 GLY D  488  GLN D  518  1                                  31    
HELIX   92 AK2 ASP D  521  HIS D  541  1                                  21    
HELIX   93 AK3 PRO D  544  TYR D  559  1                                  16    
HELIX   94 AK4 ASP D  565  LEU D  573  1                                   9    
HELIX   95 AK5 SER D  574  ALA D  591  1                                  18    
HELIX   96 AK6 ASP D  600  LEU D  608  1                                   9    
HELIX   97 AK7 THR D  609  LEU D  611  5                                   3    
HELIX   98 AK8 GLU D  660  ARG D  666  1                                   7    
HELIX   99 AK9 VAL D  686  TYR D  696  1                                  11    
HELIX  100 AL1 TYR D  696  LEU D  708  1                                  13    
SHEET    1 AA1 4 ARG A 612  PHE A 616  0                                        
SHEET    2 AA1 4 CYS A 679  SER A 685 -1  O  LEU A 681   N  GLU A 614           
SHEET    3 AA1 4 LYS A 631  HIS A 637 -1  N  PHE A 634   O  TYR A 682           
SHEET    4 AA1 4 TYR A 657  PHE A 658 -1  O  PHE A 658   N  TYR A 633           
SHEET    1 AA2 4 TYR A 621  ILE A 623  0                                        
SHEET    2 AA2 4 SER A 672  ALA A 675 -1  O  VAL A 673   N  ILE A 623           
SHEET    3 AA2 4 VAL A 640  THR A 644 -1  N  SER A 641   O  ARG A 674           
SHEET    4 AA2 4 LYS A 648  LEU A 652 -1  O  LEU A 652   N  VAL A 640           
SHEET    1 AA3 4 ARG B 612  PHE B 616  0                                        
SHEET    2 AA3 4 CYS B 679  SER B 685 -1  O  LEU B 681   N  GLU B 614           
SHEET    3 AA3 4 LYS B 631  HIS B 637 -1  N  PHE B 634   O  TYR B 682           
SHEET    4 AA3 4 TYR B 657  PHE B 658 -1  O  PHE B 658   N  TYR B 633           
SHEET    1 AA4 4 TYR B 621  ILE B 623  0                                        
SHEET    2 AA4 4 SER B 672  ALA B 675 -1  O  VAL B 673   N  ILE B 623           
SHEET    3 AA4 4 VAL B 640  THR B 644 -1  N  SER B 641   O  ARG B 674           
SHEET    4 AA4 4 LYS B 648  LEU B 652 -1  O  LEU B 652   N  VAL B 640           
SHEET    1 AA5 4 ARG C 612  PHE C 616  0                                        
SHEET    2 AA5 4 CYS C 679  SER C 685 -1  O  LEU C 681   N  GLU C 614           
SHEET    3 AA5 4 LYS C 631  HIS C 637 -1  N  PHE C 634   O  TYR C 682           
SHEET    4 AA5 4 TYR C 657  PHE C 658 -1  O  PHE C 658   N  TYR C 633           
SHEET    1 AA6 4 TYR C 621  ILE C 623  0                                        
SHEET    2 AA6 4 SER C 672  ALA C 675 -1  O  VAL C 673   N  ILE C 623           
SHEET    3 AA6 4 VAL C 640  THR C 644 -1  N  SER C 641   O  ARG C 674           
SHEET    4 AA6 4 LYS C 648  LEU C 652 -1  O  LEU C 652   N  VAL C 640           
SHEET    1 AA7 4 ARG D 612  PHE D 616  0                                        
SHEET    2 AA7 4 CYS D 679  SER D 685 -1  O  LEU D 681   N  GLU D 614           
SHEET    3 AA7 4 LYS D 631  HIS D 637 -1  N  PHE D 634   O  TYR D 682           
SHEET    4 AA7 4 TYR D 657  PHE D 658 -1  O  PHE D 658   N  TYR D 633           
SHEET    1 AA8 4 TYR D 621  ILE D 623  0                                        
SHEET    2 AA8 4 SER D 672  ALA D 675 -1  O  VAL D 673   N  ILE D 623           
SHEET    3 AA8 4 VAL D 640  THR D 644 -1  N  SER D 641   O  ARG D 674           
SHEET    4 AA8 4 LYS D 648  LEU D 652 -1  O  LEU D 652   N  VAL D 640           
CISPEP   1 GLY A  480    TYR A  481          0       -21.88                     
CISPEP   2 GLY B  480    TYR B  481          0       -21.82                     
CISPEP   3 GLY C  480    TYR C  481          0       -21.79                     
CISPEP   4 GLY D  480    TYR D  481          0       -21.80                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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