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Database: PDB
Entry: 6B8N
LinkDB: 6B8N
Original site: 6B8N 
HEADER    METAL TRANSPORT                         09-OCT-17   6B8N              
TITLE     CRYSTAL STRUCTURE OF THE CA2+/CAM:KV7.4 (KCNQ4) AB DOMAIN COMPLEX, 10 
TITLE    2 UM CACL2 SOAK                                                        
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,D.L.MINOR                                                     
REVDAT   3   04-OCT-23 6B8N    1       LINK                                     
REVDAT   2   11-DEC-19 6B8N    1       REMARK                                   
REVDAT   1   14-MAR-18 6B8N    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 CA                                       
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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 64572                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1993                            
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 14.9773 -  5.2337    1.00     4684   150  0.1734 0.2081        
REMARK   3     2  5.2337 -  4.1839    1.00     4543   145  0.1736 0.2305        
REMARK   3     3  4.1839 -  3.6639    1.00     4520   143  0.1789 0.2330        
REMARK   3     4  3.6639 -  3.3329    1.00     4498   145  0.2046 0.2637        
REMARK   3     5  3.3329 -  3.0963    1.00     4467   141  0.2319 0.2598        
REMARK   3     6  3.0963 -  2.9152    1.00     4471   144  0.2459 0.3072        
REMARK   3     7  2.9152 -  2.7701    1.00     4448   142  0.2466 0.2750        
REMARK   3     8  2.7701 -  2.6502    1.00     4433   141  0.2748 0.3204        
REMARK   3     9  2.6502 -  2.5487    1.00     4467   142  0.2753 0.3146        
REMARK   3    10  2.5487 -  2.4612    0.99     4419   141  0.2966 0.3272        
REMARK   3    11  2.4612 -  2.3845    0.99     4399   140  0.3215 0.3503        
REMARK   3    12  2.3845 -  2.3166    0.99     4440   140  0.3320 0.3687        
REMARK   3    13  2.3166 -  2.2558    1.00     4392   140  0.3504 0.3811        
REMARK   3    14  2.2558 -  2.2010    0.99     4398   139  0.3903 0.3930        
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) : 32.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.15                          
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      :  0.002           7235                                  
REMARK   3   ANGLE     :  0.419           9708                                  
REMARK   3   CHIRALITY :  0.036           1063                                  
REMARK   3   PLANARITY :  0.003           1267                                  
REMARK   3   DIHEDRAL  : 23.010           2778                                  
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 6B8N 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_1000230457.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL KHOZU       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124961                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.977                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.520                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.42                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.34500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.720                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6B8L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M BISTRIS PH     
REMARK 280  6.5, 0.01MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  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       54.14950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.69100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       82.23450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.14950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.69100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.23450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.14950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       71.69100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.23450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.14950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       71.69100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.23450            
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: 4110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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: 4060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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: 4410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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: 4380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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     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     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     LYS D   148                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     HIS E   323                                                      
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     HIS G   330                                                      
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 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    MET A 357       -6.86   -143.14                                   
REMARK 500    LEU A 362       55.63    -97.26                                   
REMARK 500    MET A 527       87.57   -156.94                                   
REMARK 500    ASP B  20       73.88    -67.58                                   
REMARK 500    LYS B  75     -113.21     53.06                                   
REMARK 500    ASN B 137       93.26    -62.67                                   
REMARK 500    PHE C 335        0.05    -69.89                                   
REMARK 500    LEU C 362       50.52   -102.51                                   
REMARK 500    LYS D  75     -117.31     51.89                                   
REMARK 500    GLU D 114       89.51    -67.30                                   
REMARK 500    MET E 357       -4.76   -140.19                                   
REMARK 500    LEU E 362       56.41    -94.11                                   
REMARK 500    LYS F  75     -119.25     57.30                                   
REMARK 500    LEU G 362       50.68    -96.16                                   
REMARK 500    LYS H  75     -118.78     56.25                                   
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 B 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  20   OD1                                                    
REMARK 620 2 ASP B  22   OD1  73.9                                              
REMARK 620 3 ASP B  24   OD1  74.4  78.9                                        
REMARK 620 4 THR B  26   O    73.2 144.9  80.8                                  
REMARK 620 5 GLU B  31   OE1  89.7  85.8 160.5 105.8                            
REMARK 620 6 GLU B  31   OE2 114.9 136.4 144.3  70.4  53.2                      
REMARK 620 7 HOH B 305   O   162.1  90.6  94.1 119.3  98.2  82.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  20   OD1                                                    
REMARK 620 2 ASP D  22   OD1  66.1                                              
REMARK 620 3 ASP D  24   OD1  69.4  77.1                                        
REMARK 620 4 THR D  26   O    70.7 136.4  83.0                                  
REMARK 620 5 GLU D  31   OE1  98.3 123.8 150.3  67.3                            
REMARK 620 6 GLU D  31   OE2  91.2  73.9 149.9 113.0  51.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  20   OD2                                                    
REMARK 620 2 ASP F  22   OD1  65.0                                              
REMARK 620 3 ASP F  22   OD2 108.9  43.9                                        
REMARK 620 4 ASP F  24   OD1  67.4  71.3  85.3                                  
REMARK 620 5 THR F  26   O    67.5 131.9 169.3  84.1                            
REMARK 620 6 GLU F  31   OE1 103.2 127.3 119.6 155.0  71.0                      
REMARK 620 7 GLU F  31   OE2  89.3  75.0  77.5 144.7 112.1  52.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  20   OD2                                                    
REMARK 620 2 ASP H  22   OD2  68.7                                              
REMARK 620 3 ASP H  24   OD1  72.7  74.6                                        
REMARK 620 4 THR H  26   O    74.3 140.9  82.8                                  
REMARK 620 5 GLU H  31   OE1  98.3 128.4 151.3  68.5                            
REMARK 620 6 GLU H  31   OE2  90.2  77.8 151.3 115.2  51.8                      
REMARK 620 7 HOH H 313   O   164.7  97.0  98.8 118.0  95.0  92.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 202                 
DBREF  6B8N A  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8N A  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8N B    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8N C  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8N C  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8N D    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8N E  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8N E  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8N F    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6B8N G  325   367  UNP    P56696   KCNQ4_HUMAN    325    367             
DBREF  6B8N G  524   557  UNP    P56696   KCNQ4_HUMAN    524    557             
DBREF  6B8N H    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
SEQADV 6B8N GLY A  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N HIS A  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N MET A  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N LYS A  368  UNP  P56696              LINKER                         
SEQADV 6B8N LEU A  369  UNP  P56696              LINKER                         
SEQADV 6B8N GLY C  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N HIS C  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N MET C  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N LYS C  368  UNP  P56696              LINKER                         
SEQADV 6B8N LEU C  369  UNP  P56696              LINKER                         
SEQADV 6B8N GLY E  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N HIS E  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N MET E  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N LYS E  368  UNP  P56696              LINKER                         
SEQADV 6B8N LEU E  369  UNP  P56696              LINKER                         
SEQADV 6B8N GLY G  322  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N HIS G  323  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N MET G  324  UNP  P56696              EXPRESSION TAG                 
SEQADV 6B8N LYS G  368  UNP  P56696              LINKER                         
SEQADV 6B8N 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     CA  B 201       1                                                       
HET    SO4  C 601       5                                                       
HET    SO4  C 602       5                                                       
HET     CA  D 201       1                                                       
HET     CA  F 201       1                                                       
HET    SO4  F 202       5                                                       
HET     CA  H 201       1                                                       
HET    SO4  H 202       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9   CA    4(CA 2+)                                                     
FORMUL  10  SO4    4(O4 S 2-)                                                   
FORMUL  17  HOH   *293(H2 O)                                                    
HELIX    1 AA1 LYS A  325  LYS A  337  1                                  13    
HELIX    2 AA2 ARG A  338  THR A  355  1                                  18    
HELIX    3 AA3 ASP A  356  MET A  357  5                                   2    
HELIX    4 AA4 SER A  358  LEU A  362  5                                   5    
HELIX    5 AA5 THR A  363  MET A  527  1                                  11    
HELIX    6 AA6 PRO A  528  GLU A  551  1                                  24    
HELIX    7 AA7 THR B    5  ASP B   20  1                                  16    
HELIX    8 AA8 THR B   28  LEU B   39  1                                  12    
HELIX    9 AA9 THR B   44  GLU B   54  1                                  11    
HELIX   10 AB1 PHE B   65  LYS B   75  1                                  11    
HELIX   11 AB2 ASP B   78  VAL B   91  1                                  14    
HELIX   12 AB3 ALA B  102  THR B  110  1                                   9    
HELIX   13 AB4 THR B  117  ALA B  128  1                                  12    
HELIX   14 AB5 TYR B  138  THR B  146  1                                   9    
HELIX   15 AB6 VAL C  326  ARG C  338  1                                  13    
HELIX   16 AB7 ARG C  338  THR C  355  1                                  18    
HELIX   17 AB8 ASP C  356  MET C  357  5                                   2    
HELIX   18 AB9 SER C  358  LEU C  362  5                                   5    
HELIX   19 AC1 THR C  363  MET C  527  1                                  11    
HELIX   20 AC2 PRO C  528  GLU C  551  1                                  24    
HELIX   21 AC3 THR D    5  ASP D   20  1                                  16    
HELIX   22 AC4 THR D   28  LEU D   39  1                                  12    
HELIX   23 AC5 THR D   44  ASP D   56  1                                  13    
HELIX   24 AC6 PHE D   65  LYS D   75  1                                  11    
HELIX   25 AC7 ASP D   78  PHE D   92  1                                  15    
HELIX   26 AC8 ALA D  102  LEU D  112  1                                  11    
HELIX   27 AC9 THR D  117  ASP D  129  1                                  13    
HELIX   28 AD1 TYR D  138  THR D  146  1                                   9    
HELIX   29 AD2 LYS E  325  HIS E  334  1                                  10    
HELIX   30 AD3 HIS E  334  THR E  355  1                                  22    
HELIX   31 AD4 ASP E  356  MET E  357  5                                   2    
HELIX   32 AD5 SER E  358  LEU E  362  5                                   5    
HELIX   33 AD6 THR E  363  MET E  527  1                                  11    
HELIX   34 AD7 PRO E  528  GLU E  551  1                                  24    
HELIX   35 AD8 GLU F    6  ASP F   20  1                                  15    
HELIX   36 AD9 THR F   28  LEU F   39  1                                  12    
HELIX   37 AE1 THR F   44  GLU F   54  1                                  11    
HELIX   38 AE2 PHE F   65  LYS F   75  1                                  11    
HELIX   39 AE3 ASP F   78  VAL F   91  1                                  14    
HELIX   40 AE4 ALA F  102  LEU F  112  1                                  11    
HELIX   41 AE5 THR F  117  ALA F  128  1                                  12    
HELIX   42 AE6 ASN F  137  THR F  146  1                                  10    
HELIX   43 AE7 HIS G  334  THR G  355  1                                  22    
HELIX   44 AE8 ASP G  356  MET G  357  5                                   2    
HELIX   45 AE9 SER G  358  LEU G  362  5                                   5    
HELIX   46 AF1 THR G  363  MET G  527  1                                  11    
HELIX   47 AF2 PRO G  528  GLU G  551  1                                  24    
HELIX   48 AF3 THR H    5  ASP H   20  1                                  16    
HELIX   49 AF4 THR H   28  LEU H   39  1                                  12    
HELIX   50 AF5 THR H   44  GLU H   54  1                                  11    
HELIX   51 AF6 PHE H   65  LYS H   75  1                                  11    
HELIX   52 AF7 ASP H   78  PHE H   92  1                                  15    
HELIX   53 AF8 ALA H  102  LEU H  112  1                                  11    
HELIX   54 AF9 THR H  117  ALA H  128  1                                  12    
HELIX   55 AG1 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 THR F  26  ILE F  27  0                                        
SHEET    2 AA5 2 ILE F  63  ASP F  64 -1  O  ILE F  63   N  ILE F  27           
SHEET    1 AA6 3 ILE F 100  SER F 101  0                                        
SHEET    2 AA6 3 GLN F 135  VAL F 136 -1  O  VAL F 136   N  ILE F 100           
SHEET    3 AA6 3 ILE F 130  ASP F 131 -1  N  ASP F 131   O  GLN F 135           
SHEET    1 AA7 2 THR H  26  ILE H  27  0                                        
SHEET    2 AA7 2 ILE H  63  ASP H  64 -1  O  ILE H  63   N  ILE H  27           
SHEET    1 AA8 3 TYR H  99  SER H 101  0                                        
SHEET    2 AA8 3 GLN H 135  ASN H 137 -1  O  VAL H 136   N  ILE H 100           
SHEET    3 AA8 3 ILE H 130  ASP H 131 -1  N  ASP H 131   O  GLN H 135           
LINK         OD1 ASP B  20                CA    CA B 201     1555   1555  2.47  
LINK         OD1 ASP B  22                CA    CA B 201     1555   1555  2.39  
LINK         OD1 ASP B  24                CA    CA B 201     1555   1555  2.36  
LINK         O   THR B  26                CA    CA B 201     1555   1555  2.54  
LINK         OE1 GLU B  31                CA    CA B 201     1555   1555  2.44  
LINK         OE2 GLU B  31                CA    CA B 201     1555   1555  2.47  
LINK        CA    CA B 201                 O   HOH B 305     1555   1555  2.50  
LINK         OD1 ASP D  20                CA    CA D 201     1555   1555  2.54  
LINK         OD1 ASP D  22                CA    CA D 201     1555   1555  2.50  
LINK         OD1 ASP D  24                CA    CA D 201     1555   1555  2.37  
LINK         O   THR D  26                CA    CA D 201     1555   1555  2.52  
LINK         OE1 GLU D  31                CA    CA D 201     1555   1555  2.58  
LINK         OE2 GLU D  31                CA    CA D 201     1555   1555  2.43  
LINK         OD2 ASP F  20                CA    CA F 201     1555   1555  2.72  
LINK         OD1 ASP F  22                CA    CA F 201     1555   1555  2.51  
LINK         OD2 ASP F  22                CA    CA F 201     1555   1555  3.14  
LINK         OD1 ASP F  24                CA    CA F 201     1555   1555  2.33  
LINK         O   THR F  26                CA    CA F 201     1555   1555  2.52  
LINK         OE1 GLU F  31                CA    CA F 201     1555   1555  2.47  
LINK         OE2 GLU F  31                CA    CA F 201     1555   1555  2.47  
LINK         OD2 ASP H  20                CA    CA H 201     1555   1555  2.49  
LINK         OD2 ASP H  22                CA    CA H 201     1555   1555  2.47  
LINK         OD1 ASP H  24                CA    CA H 201     1555   1555  2.33  
LINK         O   THR H  26                CA    CA H 201     1555   1555  2.50  
LINK         OE1 GLU H  31                CA    CA H 201     1555   1555  2.52  
LINK         OE2 GLU H  31                CA    CA H 201     1555   1555  2.53  
LINK        CA    CA H 201                 O   HOH H 313     1555   1555  2.48  
SITE     1 AC1  6 ASP B  20  ASP B  22  ASP B  24  THR B  26                    
SITE     2 AC1  6 GLU B  31  HOH B 305                                          
SITE     1 AC2  5 THR C 363  ALA C 364  HOH C 716  LYS F  21                    
SITE     2 AC2  5 TYR G 367                                                     
SITE     1 AC3  4 ARG C 359  ARG D 126  ARG G 359  ARG H 126                    
SITE     1 AC4  5 ASP D  20  ASP D  22  ASP D  24  THR D  26                    
SITE     2 AC4  5 GLU D  31                                                     
SITE     1 AC5  5 ASP F  20  ASP F  22  ASP F  24  THR F  26                    
SITE     2 AC5  5 GLU F  31                                                     
SITE     1 AC6  5 GLN D  41  ASN D  42  GLN F  41  ASN F  42                    
SITE     2 AC6  5 HOH F 327                                                     
SITE     1 AC7  6 ASP H  20  ASP H  22  ASP H  24  THR H  26                    
SITE     2 AC7  6 GLU H  31  HOH H 313                                          
SITE     1 AC8  4 GLN B  41  ASN B  42  GLN H  41  ASN H  42                    
CRYST1  108.299  143.382  164.469  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      0.009234  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006974  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006080        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system