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Database: PDB
Entry: 6N5W
LinkDB: 6N5W
Original site: 6N5W 
HEADER    METAL BINDING PROTEIN                   22-NOV-18   6N5W              
TITLE     CRYSTAL STRUCTURE OF THE CA2+/CAM COMPLEX WITH INDEPENDENT PEPTIDES OF
TITLE    2 KV7.4 (KCNQ4) A & B DOMAINS                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: KQT-LIKE 4,POTASSIUM CHANNEL SUBUNIT ALPHA KVLQT4,VOLTAGE-  
COMPND   5 GATED POTASSIUM CHANNEL SUBUNIT KV7.4;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;    
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: KQT-LIKE 4,POTASSIUM CHANNEL SUBUNIT ALPHA KVLQT4,VOLTAGE-  
COMPND  11 GATED POTASSIUM CHANNEL SUBUNIT KV7.4;                               
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CALMODULIN-1;                                              
COMPND  15 CHAIN: C;                                                            
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PETGQ.HCAM                                
KEYWDS    ION CHANNEL, CALMODULIN, KCNQ4 PEPTIDES, COMPLEX, METAL BINDING       
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.TAYLOR,C.R.ARCHER,M.S.SHAPIRO                                     
REVDAT   4   11-OCT-23 6N5W    1       REMARK                                   
REVDAT   3   04-DEC-19 6N5W    1       REMARK                                   
REVDAT   2   24-APR-19 6N5W    1       JRNL                                     
REVDAT   1   13-MAR-19 6N5W    0                                                
JRNL        AUTH   C.R.ARCHER,B.T.ENSLOW,A.B.TAYLOR,V.DE LA ROSA,               
JRNL        AUTH 2 A.BHATTACHARYA,M.S.SHAPIRO                                   
JRNL        TITL   A MUTUALLY INDUCED CONFORMATIONAL FIT UNDERLIES              
JRNL        TITL 2 CA2+-DIRECTED INTERACTIONS BETWEEN CALMODULIN AND THE        
JRNL        TITL 3 PROXIMAL C TERMINUS OF KCNQ4 K+CHANNELS.                     
JRNL        REF    J. BIOL. CHEM.                V. 294  6094 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30808708                                                     
JRNL        DOI    10.1074/JBC.RA118.006857                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11810                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1179                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.2861 -  4.2986    0.99     1416   176  0.1965 0.2035        
REMARK   3     2  4.2986 -  3.4124    1.00     1386   118  0.1943 0.2694        
REMARK   3     3  3.4124 -  2.9812    1.00     1281   177  0.2612 0.3274        
REMARK   3     4  2.9812 -  2.7087    1.00     1360   118  0.2710 0.3411        
REMARK   3     5  2.7087 -  2.5146    1.00     1284   177  0.2796 0.3513        
REMARK   3     6  2.5146 -  2.3664    1.00     1319   118  0.2990 0.2985        
REMARK   3     7  2.3664 -  2.2479    1.00     1259   177  0.3181 0.3433        
REMARK   3     8  2.2479 -  2.1500    1.00     1326   118  0.3425 0.3921        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           1514                                  
REMARK   3   ANGLE     :  1.127           2032                                  
REMARK   3   CHIRALITY :  0.077            227                                  
REMARK   3   PLANARITY :  0.005            269                                  
REMARK   3   DIHEDRAL  : 23.281            581                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 356 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6051  20.8231  -5.8396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5073 T22:   0.3210                                     
REMARK   3      T33:   0.2434 T12:   0.1133                                     
REMARK   3      T13:  -0.0137 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0106 L22:   1.3045                                     
REMARK   3      L33:   0.4599 L12:   0.8776                                     
REMARK   3      L13:  -0.4319 L23:  -0.4832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2658 S12:   0.0964 S13:  -0.1637                       
REMARK   3      S21:  -0.3948 S22:   0.6325 S23:  -0.0231                       
REMARK   3      S31:  -0.3436 S32:  -0.5646 S33:   0.1366                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 525 THROUGH 549 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0423  10.4558  -9.6824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3744 T22:   0.3747                                     
REMARK   3      T33:   0.3050 T12:  -0.0352                                     
REMARK   3      T13:   0.0123 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2397 L22:   0.1502                                     
REMARK   3      L33:   0.3399 L12:  -0.1532                                     
REMARK   3      L13:  -0.2043 L23:   0.2242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1014 S12:   0.0503 S13:   0.0095                       
REMARK   3      S21:   0.5764 S22:  -0.3538 S23:  -0.4282                       
REMARK   3      S31:  -0.1181 S32:  -0.0542 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 78 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1494   6.1267 -15.8142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2917 T22:   0.3491                                     
REMARK   3      T33:   0.3907 T12:  -0.0269                                     
REMARK   3      T13:   0.0384 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7814 L22:   1.0201                                     
REMARK   3      L33:   0.7380 L12:  -0.1787                                     
REMARK   3      L13:  -0.5766 L23:   0.4042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0631 S12:   0.2590 S13:   0.0710                       
REMARK   3      S21:   0.1034 S22:  -0.0651 S23:  -0.2743                       
REMARK   3      S31:  -0.0882 S32:   0.0030 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 79 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6985  25.8706   1.7816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6673 T22:   0.4170                                     
REMARK   3      T33:   0.5055 T12:   0.1321                                     
REMARK   3      T13:   0.1625 T23:   0.2392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6641 L22:   0.5847                                     
REMARK   3      L33:   4.5717 L12:  -0.2153                                     
REMARK   3      L13:  -0.5771 L23:   0.9296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4137 S12:  -0.1814 S13:   0.1446                       
REMARK   3      S21:   0.2120 S22:   0.2725 S23:   0.1581                       
REMARK   3      S31:  -1.3472 S32:  -0.2506 S33:   2.0627                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6N5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238239.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 1.07300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4UMO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M SODIUM CITRATE, 0.1 M HEPES PH     
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       21.75500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.28500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.75500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.28500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     GLU A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     MET A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     ALA A   360                                                      
REMARK 465     TYR A   361                                                      
REMARK 465     LEU A   362                                                      
REMARK 465     ASP B   524                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     LYS C   148                                                      
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 C  75     -124.87     52.33                                   
REMARK 500    ARG C  90      -37.45    -37.36                                   
REMARK 500    ASN C 137       93.38    -68.59                                   
REMARK 500    THR C 146       54.44    -91.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  20   OD1                                                    
REMARK 620 2 ASP C  22   OD1  71.6                                              
REMARK 620 3 ASP C  24   OD1  77.5  74.8                                        
REMARK 620 4 THR C  26   O    87.8 152.0  82.5                                  
REMARK 620 5 GLU C  31   OE1  96.8  81.9 156.7 120.2                            
REMARK 620 6 GLU C  31   OE2 117.9 132.1 150.9  74.1  51.3                      
REMARK 620 7 HOH C 307   O   154.0  84.5  86.8 110.7  89.5  85.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  56   OD1                                                    
REMARK 620 2 ASP C  58   OD1  72.2                                              
REMARK 620 3 ASN C  60   OD1  81.6  76.4                                        
REMARK 620 4 THR C  62   O    80.5 149.2  86.0                                  
REMARK 620 5 GLU C  67   OE1  99.8 115.0 168.5  83.0                            
REMARK 620 6 GLU C  67   OE2  88.3  66.6 142.9 127.5  48.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
DBREF  6N5W A  336   362  UNP    P56696   KCNQ4_HUMAN    336    362             
DBREF  6N5W B  524   549  UNP    P56696   KCNQ4_HUMAN    470    495             
DBREF  6N5W C    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
SEQRES   1 A   27  GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN ALA          
SEQRES   2 A   27  ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA TYR          
SEQRES   3 A   27  LEU                                                          
SEQRES   1 B   26  ASP ASP ILE MET PRO ALA VAL LYS THR VAL ILE ARG SER          
SEQRES   2 B   26  ILE ARG ILE LEU LYS PHE LEU VAL ALA LYS ARG LYS PHE          
SEQRES   1 C  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 C  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 C  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 C  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 C  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  149  GLN MET MET THR ALA LYS                                      
HET     CA  C 201       1                                                       
HET     CA  C 202       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HOH   *23(H2 O)                                                     
HELIX    1 AA1 ARG A  338  SER A  354  1                                  17    
HELIX    2 AA2 ILE B  526  PHE B  549  1                                  24    
HELIX    3 AA3 THR C    5  ASP C   20  1                                  16    
HELIX    4 AA4 THR C   28  LEU C   39  1                                  12    
HELIX    5 AA5 THR C   44  ASP C   56  1                                  13    
HELIX    6 AA6 PHE C   65  LYS C   75  1                                  11    
HELIX    7 AA7 ASP C   80  VAL C   91  1                                  12    
HELIX    8 AA8 ALA C  102  LEU C  112  1                                  11    
HELIX    9 AA9 THR C  117  ASP C  129  1                                  13    
HELIX   10 AB1 TYR C  138  THR C  146  1                                   9    
SHEET    1 AA1 2 THR C  26  ILE C  27  0                                        
SHEET    2 AA1 2 ILE C  63  ASP C  64 -1  O  ILE C  63   N  ILE C  27           
SHEET    1 AA2 2 TYR C  99  SER C 101  0                                        
SHEET    2 AA2 2 GLN C 135  ASN C 137 -1  O  VAL C 136   N  ILE C 100           
LINK         OD1 ASP C  20                CA    CA C 201     1555   1555  2.44  
LINK         OD1 ASP C  22                CA    CA C 201     1555   1555  2.16  
LINK         OD1 ASP C  24                CA    CA C 201     1555   1555  2.55  
LINK         O   THR C  26                CA    CA C 201     1555   1555  2.30  
LINK         OE1 GLU C  31                CA    CA C 201     1555   1555  2.68  
LINK         OE2 GLU C  31                CA    CA C 201     1555   1555  2.35  
LINK         OD1 ASP C  56                CA    CA C 202     1555   1555  2.42  
LINK         OD1 ASP C  58                CA    CA C 202     1555   1555  2.48  
LINK         OD1 ASN C  60                CA    CA C 202     1555   1555  2.50  
LINK         O   THR C  62                CA    CA C 202     1555   1555  2.48  
LINK         OE1 GLU C  67                CA    CA C 202     1555   1555  2.63  
LINK         OE2 GLU C  67                CA    CA C 202     1555   1555  2.70  
LINK        CA    CA C 201                 O   HOH C 307     1555   1555  2.70  
SITE     1 AC1  6 ASP C  20  ASP C  22  ASP C  24  THR C  26                    
SITE     2 AC1  6 GLU C  31  HOH C 307                                          
SITE     1 AC2  5 ASP C  56  ASP C  58  ASN C  60  THR C  62                    
SITE     2 AC2  5 GLU C  67                                                     
CRYST1   43.510  130.570   36.160  90.00  90.00  90.00 P 21 21 2     4          
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      0.022983  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007659  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027655        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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