GenomeNet

Database: PDB
Entry: 6B8L
LinkDB: 6B8L
Original site: 6B8L 
HEADER    METAL TRANSPORT                         09-OCT-17   6B8L              
TITLE     CRYSTAL STRUCTURE OF THE APO/CAM:KV7.4 (KCNQ4) AB DOMAIN COMPLEX      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;    
COMPND   3 CHAIN: A, C, E, G;                                                   
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: CALMODULIN-1;                                              
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 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: KCNQ4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
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;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PEGST                                     
KEYWDS    ION CHANNEL, COMPLEX, METAL TRANSPORT                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHANG,F.ABDEREMANE-ALI,D.L.MINOR                                    
REVDAT   3   13-MAR-24 6B8L    1       REMARK                                   
REVDAT   2   18-DEC-19 6B8L    1       REMARK                                   
REVDAT   1   14-MAR-18 6B8L    0                                                
JRNL        AUTH   A.CHANG,F.ABDEREMANE-ALI,G.L.HURA,N.D.ROSSEN,R.E.GATE,       
JRNL        AUTH 2 D.L.MINOR                                                    
JRNL        TITL   A CALMODULIN C-LOBE CA2+-DEPENDENT SWITCH GOVERNS KV7        
JRNL        TITL 2 CHANNEL FUNCTION                                             
JRNL        REF    NEURON                        V.  97   836 2018              
JRNL        REFN                   ISSN 1097-4199                               
JRNL        PMID   29429937                                                     
JRNL        DOI    10.1016/J.NEURON.2018.01.035                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 54987                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5475                            
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 48.8996 -  7.0852    0.99     1859   207  0.1708 0.1846        
REMARK   3     2  7.0852 -  5.6264    1.00     1801   201  0.2109 0.2411        
REMARK   3     3  5.6264 -  4.9159    1.00     1768   195  0.1840 0.2285        
REMARK   3     4  4.9159 -  4.4668    1.00     1762   196  0.1618 0.1906        
REMARK   3     5  4.4668 -  4.1468    1.00     1762   197  0.1531 0.2039        
REMARK   3     6  4.1468 -  3.9025    0.99     1711   191  0.1701 0.2187        
REMARK   3     7  3.9025 -  3.7071    0.99     1731   196  0.1800 0.2262        
REMARK   3     8  3.7071 -  3.5458    0.98     1709   189  0.2196 0.2603        
REMARK   3     9  3.5458 -  3.4093    0.99     1728   193  0.1992 0.2632        
REMARK   3    10  3.4093 -  3.2917    0.99     1708   190  0.2149 0.2607        
REMARK   3    11  3.2917 -  3.1888    0.99     1722   193  0.2194 0.2653        
REMARK   3    12  3.1888 -  3.0976    0.99     1720   190  0.2280 0.2601        
REMARK   3    13  3.0976 -  3.0161    0.99     1715   191  0.2200 0.2818        
REMARK   3    14  3.0161 -  2.9425    0.98     1723   191  0.2259 0.2634        
REMARK   3    15  2.9425 -  2.8756    0.97     1679   186  0.2227 0.2899        
REMARK   3    16  2.8756 -  2.8145    0.97     1678   186  0.2151 0.3154        
REMARK   3    17  2.8145 -  2.7582    0.96     1646   181  0.2223 0.2612        
REMARK   3    18  2.7582 -  2.7061    0.95     1642   190  0.2330 0.2864        
REMARK   3    19  2.7061 -  2.6578    0.95     1665   183  0.2231 0.2565        
REMARK   3    20  2.6578 -  2.6127    0.95     1631   177  0.2143 0.2579        
REMARK   3    21  2.6127 -  2.5706    0.94     1610   181  0.2015 0.3178        
REMARK   3    22  2.5706 -  2.5310    0.93     1573   172  0.2194 0.2689        
REMARK   3    23  2.5310 -  2.4938    0.94     1635   178  0.2118 0.3143        
REMARK   3    24  2.4938 -  2.4587    0.92     1585   175  0.2280 0.2887        
REMARK   3    25  2.4587 -  2.4255    0.90     1554   167  0.2268 0.3202        
REMARK   3    26  2.4255 -  2.3940    0.91     1585   172  0.2311 0.2873        
REMARK   3    27  2.3940 -  2.3641    0.90     1539   168  0.2131 0.2843        
REMARK   3    28  2.3641 -  2.3356    0.90     1529   168  0.2109 0.2939        
REMARK   3    29  2.3356 -  2.3084    0.88     1528   158  0.2286 0.3058        
REMARK   3    30  2.3084 -  2.2825    0.59     1014   113  0.2108 0.2842        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.03                          
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      :  0.007           7074                                  
REMARK   3   ANGLE     :  0.840           9505                                  
REMARK   3   CHIRALITY :  0.047           1042                                  
REMARK   3   PLANARITY :  0.005           1239                                  
REMARK   3   DIHEDRAL  : 21.646           2713                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6B8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230454.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAR-15; 20-AUG-16               
REMARK 200  TEMPERATURE           (KELVIN) : 80; 80                             
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; APS                           
REMARK 200  BEAMLINE                       : 8.3.1; 23-ID-B                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797; 1.072                      
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111);      
REMARK 200                                   SI(111) DOUBLE CRYSTAL KHOZU       
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; PIXEL                         
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; DECTRIS         
REMARK 200                                   PILATUS 6M                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.11900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M BISTRIS PH     
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       54.21750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.22650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       82.15650            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.21750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.22650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.15650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.21750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       71.22650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.15650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.21750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       71.22650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.15650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     GLY A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     MET A   324                                                      
REMARK 465     LYS A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     GLN A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     GLN A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     ARG A   331                                                      
REMARK 465     ARG A   554                                                      
REMARK 465     PRO A   555                                                      
REMARK 465     TYR A   556                                                      
REMARK 465     ASP A   557                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     GLY C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     MET C   324                                                      
REMARK 465     LYS C   325                                                      
REMARK 465     VAL C   326                                                      
REMARK 465     GLN C   327                                                      
REMARK 465     GLU C   328                                                      
REMARK 465     GLN C   329                                                      
REMARK 465     ARG C   554                                                      
REMARK 465     PRO C   555                                                      
REMARK 465     TYR C   556                                                      
REMARK 465     ASP C   557                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D   148                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     HIS E   323                                                      
REMARK 465     MET E   324                                                      
REMARK 465     LYS E   325                                                      
REMARK 465     VAL E   326                                                      
REMARK 465     GLN E   327                                                      
REMARK 465     GLU E   328                                                      
REMARK 465     GLN E   329                                                      
REMARK 465     HIS E   330                                                      
REMARK 465     ARG E   331                                                      
REMARK 465     ARG E   554                                                      
REMARK 465     PRO E   555                                                      
REMARK 465     TYR E   556                                                      
REMARK 465     ASP E   557                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     LYS F   148                                                      
REMARK 465     GLY G   322                                                      
REMARK 465     HIS G   323                                                      
REMARK 465     MET G   324                                                      
REMARK 465     LYS G   325                                                      
REMARK 465     VAL G   326                                                      
REMARK 465     GLN G   327                                                      
REMARK 465     GLU G   328                                                      
REMARK 465     GLN G   329                                                      
REMARK 465     PRO G   555                                                      
REMARK 465     TYR G   556                                                      
REMARK 465     ASP G   557                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     LYS H   148                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B   14   CD                                                  
REMARK 480     GLU B  114   CD                                                  
REMARK 480     GLU D   11   CD                                                  
REMARK 480     GLU F    6   CD                                                  
REMARK 480     GLU F  104   CD                                                  
REMARK 480     GLU H    7   CD                                                  
REMARK 480     ASP H   58   CG                                                  
REMARK 480     GLU H  104   CD                                                  
REMARK 480     GLU H  123   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA F    10     OE2  GLU F    14              1.68            
REMARK 500   O    HOH E   613     O    HOH E   631              2.02            
REMARK 500   OE1  GLN H     3     O    HOH H   301              2.07            
REMARK 500   O    HOH D   311     O    HOH E   617              2.12            
REMARK 500   OD2  ASP H    58     O    HOH H   302              2.13            
REMARK 500   O    HOH D   336     O    HOH F   218              2.15            
REMARK 500   OE2  GLU H    54     O    HOH H   303              2.15            
REMARK 500   OE1  GLU E   336     O    HOH E   601              2.16            
REMARK 500   OD1  ASP B    78     O    HOH B   201              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 362       56.47    -94.83                                   
REMARK 500    LYS B  75     -119.32     54.35                                   
REMARK 500    LYS B  77       47.55    -88.71                                   
REMARK 500    THR B 146       38.67    -95.59                                   
REMARK 500    LYS D  75     -113.28     39.35                                   
REMARK 500    LYS F  75     -125.01     52.57                                   
REMARK 500    MET G 357       -1.34   -143.05                                   
REMARK 500    LEU G 362       64.29   -100.52                                   
REMARK 500    LYS H  75     -116.37     48.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 202                 
DBREF  6B8L A  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8L A  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8L B    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8L C  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8L C  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8L D    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8L E  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8L E  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8L F    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8L G  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8L G  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8L H    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
SEQADV 6B8L GLY A  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L HIS A  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L MET A  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L LYS A  368  UNP  P56696              LINKER                         
SEQADV 6B8L LEU A  369  UNP  P56696              LINKER                         
SEQADV 6B8L GLY C  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L HIS C  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L MET C  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L LYS C  368  UNP  P56696              LINKER                         
SEQADV 6B8L LEU C  369  UNP  P56696              LINKER                         
SEQADV 6B8L GLY E  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L HIS E  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L MET E  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L LYS E  368  UNP  P56696              LINKER                         
SEQADV 6B8L LEU E  369  UNP  P56696              LINKER                         
SEQADV 6B8L GLY G  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L HIS G  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L MET G  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8L LYS G  368  UNP  P56696              LINKER                         
SEQADV 6B8L LEU G  369  UNP  P56696              LINKER                         
SEQRES   1 A   82  GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS          
SEQRES   2 A   82  PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN          
SEQRES   3 A   82  ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA          
SEQRES   4 A   82  TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET          
SEQRES   5 A   82  PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU          
SEQRES   6 A   82  LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU          
SEQRES   7 A   82  ARG PRO TYR ASP                                              
SEQRES   1 B  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 B  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 B  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 B  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 B  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 B  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 B  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 B  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 B  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 B  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 B  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 B  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 C   82  GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS          
SEQRES   2 C   82  PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN          
SEQRES   3 C   82  ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA          
SEQRES   4 C   82  TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET          
SEQRES   5 C   82  PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU          
SEQRES   6 C   82  LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU          
SEQRES   7 C   82  ARG PRO TYR ASP                                              
SEQRES   1 D  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 D  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 D  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 D  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 D  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 D  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 D  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 D  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 D  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 D  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 D  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 D  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 E   82  GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS          
SEQRES   2 E   82  PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN          
SEQRES   3 E   82  ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA          
SEQRES   4 E   82  TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET          
SEQRES   5 E   82  PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU          
SEQRES   6 E   82  LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU          
SEQRES   7 E   82  ARG PRO TYR ASP                                              
SEQRES   1 F  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 F  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 F  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 F  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 F  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 F  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 F  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 F  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 F  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 F  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 F  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 F  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 G   82  GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS          
SEQRES   2 G   82  PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN          
SEQRES   3 G   82  ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA          
SEQRES   4 G   82  TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET          
SEQRES   5 G   82  PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU          
SEQRES   6 G   82  LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU          
SEQRES   7 G   82  ARG PRO TYR ASP                                              
SEQRES   1 H  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 H  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 H  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 H  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 H  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 H  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 H  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 H  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 H  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 H  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 H  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 H  149  GLN MET MET THR ALA LYS                                      
HET    SO4  D 201       5                                                       
HET    SO4  D 202       5                                                       
HET    SO4  G 601       5                                                       
HET    SO4  H 201       5                                                       
HET    SO4  H 202       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    5(O4 S 2-)                                                   
FORMUL  14  HOH   *284(H2 O)                                                    
HELIX    1 AA1 ARG A  338  THR A  355  1                                  18    
HELIX    2 AA2 ASP A  356  MET A  357  5                                   2    
HELIX    3 AA3 SER A  358  LEU A  362  5                                   5    
HELIX    4 AA4 THR A  363  MET A  527  1                                  11    
HELIX    5 AA5 PRO A  528  GLU A  551  1                                  24    
HELIX    6 AA6 THR B    5  ASP B   20  1                                  16    
HELIX    7 AA7 THR B   28  LEU B   39  1                                  12    
HELIX    8 AA8 THR B   44  GLU B   54  1                                  11    
HELIX    9 AA9 PHE B   65  LYS B   75  1                                  11    
HELIX   10 AB1 ASP B   78  PHE B   92  1                                  15    
HELIX   11 AB2 ALA B  102  LEU B  112  1                                  11    
HELIX   12 AB3 THR B  117  ALA B  128  1                                  12    
HELIX   13 AB4 TYR B  138  THR B  146  1                                   9    
HELIX   14 AB5 ARG C  331  PHE C  335  1                                   5    
HELIX   15 AB6 ARG C  338  THR C  355  1                                  18    
HELIX   16 AB7 ASP C  356  MET C  357  5                                   2    
HELIX   17 AB8 SER C  358  LEU C  362  5                                   5    
HELIX   18 AB9 THR C  363  MET C  527  1                                  11    
HELIX   19 AC1 PRO C  528  THR C  552  1                                  25    
HELIX   20 AC2 GLU D    7  ASP D   20  1                                  14    
HELIX   21 AC3 THR D   28  LEU D   39  1                                  12    
HELIX   22 AC4 THR D   44  ASP D   56  1                                  13    
HELIX   23 AC5 PHE D   65  LYS D   75  1                                  11    
HELIX   24 AC6 ASP D   78  VAL D   91  1                                  14    
HELIX   25 AC7 ALA D  102  LEU D  112  1                                  11    
HELIX   26 AC8 THR D  117  ASP D  129  1                                  13    
HELIX   27 AC9 TYR D  138  THR D  146  1                                   9    
HELIX   28 AD1 HIS E  334  SER E  354  1                                  21    
HELIX   29 AD2 SER E  358  LEU E  362  5                                   5    
HELIX   30 AD3 THR E  363  MET E  527  1                                  11    
HELIX   31 AD4 PRO E  528  GLU E  551  1                                  24    
HELIX   32 AD5 THR F    5  ASP F   20  1                                  16    
HELIX   33 AD6 THR F   28  LEU F   39  1                                  12    
HELIX   34 AD7 THR F   44  GLU F   54  1                                  11    
HELIX   35 AD8 ASP F   64  LYS F   75  1                                  12    
HELIX   36 AD9 ASP F   78  PHE F   92  1                                  15    
HELIX   37 AE1 ALA F  102  LEU F  112  1                                  11    
HELIX   38 AE2 THR F  117  ALA F  128  1                                  12    
HELIX   39 AE3 TYR F  138  THR F  146  1                                   9    
HELIX   40 AE4 HIS G  334  THR G  355  1                                  22    
HELIX   41 AE5 ASP G  356  MET G  357  5                                   2    
HELIX   42 AE6 SER G  358  LEU G  362  5                                   5    
HELIX   43 AE7 THR G  363  MET G  527  1                                  11    
HELIX   44 AE8 PRO G  528  GLU G  551  1                                  24    
HELIX   45 AE9 THR G  552  ARG G  554  5                                   3    
HELIX   46 AF1 THR H    5  ASP H   20  1                                  16    
HELIX   47 AF2 THR H   28  LEU H   39  1                                  12    
HELIX   48 AF3 THR H   44  GLU H   54  1                                  11    
HELIX   49 AF4 PHE H   65  LYS H   75  1                                  11    
HELIX   50 AF5 ASP H   78  PHE H   92  1                                  15    
HELIX   51 AF6 ALA H  102  LEU H  112  1                                  11    
HELIX   52 AF7 THR H  117  ALA H  128  1                                  12    
HELIX   53 AF8 TYR H  138  THR H  146  1                                   9    
SHEET    1 AA1 2 THR B  26  ILE B  27  0                                        
SHEET    2 AA1 2 ILE B  63  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
SHEET    1 AA2 2 TYR B  99  SER B 101  0                                        
SHEET    2 AA2 2 GLN B 135  ASN B 137 -1  O  VAL B 136   N  ILE B 100           
SHEET    1 AA3 2 THR D  26  ILE D  27  0                                        
SHEET    2 AA3 2 ILE D  63  ASP D  64 -1  O  ILE D  63   N  ILE D  27           
SHEET    1 AA4 2 TYR D  99  SER D 101  0                                        
SHEET    2 AA4 2 GLN D 135  ASN D 137 -1  O  VAL D 136   N  ILE D 100           
SHEET    1 AA5 2 TYR F  99  SER F 101  0                                        
SHEET    2 AA5 2 GLN F 135  ASN F 137 -1  O  VAL F 136   N  ILE F 100           
SHEET    1 AA6 2 THR H  26  ILE H  27  0                                        
SHEET    2 AA6 2 ILE H  63  ASP H  64 -1  O  ILE H  63   N  ILE H  27           
SHEET    1 AA7 2 TYR H  99  SER H 101  0                                        
SHEET    2 AA7 2 GLN H 135  ASN H 137 -1  O  VAL H 136   N  ILE H 100           
SITE     1 AC1  4 GLN D  41  ASN D  42  GLN F  41  ASN F  42                    
SITE     1 AC2  4 LYS D  21  LYS D  30  HOH D 311  ARG E 359                    
SITE     1 AC3  4 PHE E 335  ARG E 339  ARG G 331  PHE G 335                    
SITE     1 AC4  5 GLN B  41  ASN B  42  GLY H  40  GLN H  41                    
SITE     2 AC4  5 ASN H  42                                                     
SITE     1 AC5  2 LYS H  21  LYS H  30                                          
CRYST1  108.435  142.453  164.313  90.00  90.00  90.00 I 2 2 2      32          
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      0.009222  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007020  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system