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Database: PDB
Entry: 6MUE
LinkDB: 6MUE
Original site: 6MUE 
HEADER    CALCIUM BINDING/TRANSPORT PROTEIN       23-OCT-18   6MUE              
TITLE     VOLTAGE-GATED SODIUM CHANNEL NAV1.4 IQ DOMAIN IN COMPLEX WITH         
TITLE    2 CA2+/CALMODULIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN-1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 4 SUBUNIT ALPHA;               
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: MU-1,SKM1,SODIUM CHANNEL PROTEIN SKELETAL MUSCLE SUBUNIT    
COMPND   9 ALPHA,SODIUM CHANNEL PROTEIN TYPE IV SUBUNIT ALPHA,VOLTAGE-GATED     
COMPND  10 SODIUM CHANNEL SUBUNIT ALPHA NAV1.4;                                 
COMPND  11 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: CALM1, CALM, CAM, CAM1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: RAT;                                                
SOURCE  12 ORGANISM_TAXID: 10116                                                
KEYWDS    VOLTAGE-GATED ION CHANNEL, TRANSPORT PROTEIN, IQ DOMAIN, CALCIUM      
KEYWDS   2 BINDING-TRANSPORT PROTEIN COMPLEX                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.GARDILL,F.VAN PETEGEM                                             
REVDAT   4   08-JAN-20 6MUE    1       REMARK                                   
REVDAT   3   12-JUN-19 6MUE    1       JRNL                                     
REVDAT   2   22-MAY-19 6MUE    1       JRNL                                     
REVDAT   1   08-MAY-19 6MUE    0                                                
JRNL        AUTH   B.R.GARDILL,R.E.RIVERA-ACEVEDO,C.C.TUNG,F.VAN PETEGEM        
JRNL        TITL   CRYSTAL STRUCTURES OF CA2+-CALMODULIN BOUND TO NAVC-TERMINAL 
JRNL        TITL 2 REGIONS SUGGEST ROLE FOR EF-HAND DOMAIN IN BINDING AND       
JRNL        TITL 3 INACTIVATION.                                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 10763 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31072926                                                     
JRNL        DOI    10.1073/PNAS.1818618116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12292                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 647                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 879                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.4140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1204                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 45                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.77000                                              
REMARK   3    B22 (A**2) : -1.19000                                             
REMARK   3    B33 (A**2) : -0.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.77000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.865         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1286 ; 0.010 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  1116 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1738 ; 1.240 ; 1.664       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2624 ; 0.972 ; 1.651       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 5.564 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    79 ;30.269 ;23.671       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   234 ;14.942 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ; 7.256 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   176 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1506 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   230 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6MUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
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) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS OCTOBER 15, 2015               
REMARK 200  DATA SCALING SOFTWARE          : XDS OCTOBER 15, 2015               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14964                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.810                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.37                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.680                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4DJC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0 AND 55 % (V/V)          
REMARK 280  ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9970 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 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    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     LYS B  1716                                                      
REMARK 465     ARG B  1717                                                      
REMARK 465     LYS B  1718                                                      
REMARK 465     GLN B  1719                                                      
REMARK 465     GLU B  1720                                                      
REMARK 465     LEU B  1736                                                      
REMARK 465     GLN B  1737                                                      
REMARK 465     ARG B  1738                                                      
REMARK 465     SER B  1739                                                      
REMARK 465     VAL B  1740                                                      
REMARK 465     LYS B  1741                                                      
REMARK 465     GLN B  1742                                                      
REMARK 465     ALA B  1743                                                      
REMARK 465     SER B  1744                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     GLU A   8    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     GLU B1721    CG   CD   OE1  OE2                                  
REMARK 470     LEU B1735    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A    23     OD2  ASP A   119     1544     2.09            
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    HIS B1734       70.48     46.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 343        DISTANCE =  5.92 ANGSTROMS                       
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 A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  21   OD1                                                    
REMARK 620 2 ASP A  23   OD1  82.0                                              
REMARK 620 3 ASP A  25   OD1  81.2  81.8                                        
REMARK 620 4 THR A  27   O    78.9 154.1  78.1                                  
REMARK 620 5 GLU A  32   OE1 110.4 128.3 148.1  75.4                            
REMARK 620 6 GLU A  32   OE2 100.6  75.7 156.8 125.0  53.0                      
REMARK 620 7 HOH A 338   O   162.0  93.9  80.9  98.9  85.9  95.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   OD1                                                    
REMARK 620 2 ASP A  59   OD1  76.0                                              
REMARK 620 3 ASN A  61   OD1  88.3  76.1                                        
REMARK 620 4 THR A  63   O    87.1 150.2  79.0                                  
REMARK 620 5 GLU A  68   OE1 105.0 127.9 154.4  79.9                            
REMARK 620 6 GLU A  68   OE2  86.4  74.2 150.2 129.8  54.2                      
REMARK 620 7 HOH A 308   O   152.3  76.9  90.7 119.8  87.2  80.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  94   OD1                                                    
REMARK 620 2 ASP A  96   OD1  76.2                                              
REMARK 620 3 ASN A  98   OD1  66.2  67.5                                        
REMARK 620 4 TYR A 100   O    80.0 143.4  77.6                                  
REMARK 620 5 GLU A 105   OE1 111.0 126.6 165.3  87.7                            
REMARK 620 6 GLU A 105   OE2 101.0  71.9 139.3 140.6  54.7                      
REMARK 620 7 HOH A 329   O   178.0 101.8 113.3 101.9  70.0  78.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 130   OD1                                                    
REMARK 620 2 ASP A 132   OD1  80.5                                              
REMARK 620 3 ASP A 134   OD1  82.8  74.6                                        
REMARK 620 4 GLN A 136   O    94.2 149.9  75.4                                  
REMARK 620 5 GLN A 136   O    83.4 151.1  79.8  12.3                            
REMARK 620 6 GLU A 141   OE1 115.5 124.4 154.2  84.8  84.2                      
REMARK 620 7 GLU A 141   OE2  91.7  75.4 150.0 134.6 129.0  52.6                
REMARK 620 8 HOH A 326   O   160.6  83.8  82.0  93.6 105.7  82.9  95.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 204                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6MUD   RELATED DB: PDB                                   
DBREF  6MUE A    1   149  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6MUE B 1716  1744  UNP    P15390   SCN4A_RAT     1716   1744             
SEQADV 6MUE GLY A   -1  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6MUE HIS A    0  UNP  P0DP23              EXPRESSION TAG                 
SEQRES   1 A  151  GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA          
SEQRES   2 A  151  GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY          
SEQRES   3 A  151  ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET          
SEQRES   4 A  151  ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN          
SEQRES   5 A  151  ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR          
SEQRES   6 A  151  ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS          
SEQRES   7 A  151  MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA          
SEQRES   8 A  151  PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER          
SEQRES   9 A  151  ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU          
SEQRES  10 A  151  LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU          
SEQRES  11 A  151  ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU          
SEQRES  12 A  151  PHE VAL GLN MET MET THR ALA LYS                              
SEQRES   1 B   29  LYS ARG LYS GLN GLU GLU VAL CYS ALA ILE LYS ILE GLN          
SEQRES   2 B   29  ARG ALA TYR ARG ARG HIS LEU LEU GLN ARG SER VAL LYS          
SEQRES   3 B   29  GLN ALA SER                                                  
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *45(H2 O)                                                     
HELIX    1 AA1 GLU A    8  ASP A   21  1                                  14    
HELIX    2 AA2 THR A   29  LEU A   40  1                                  12    
HELIX    3 AA3 THR A   45  ASP A   57  1                                  13    
HELIX    4 AA4 PHE A   66  ASP A   94  1                                  29    
HELIX    5 AA5 SER A  102  ASN A  112  1                                  11    
HELIX    6 AA6 THR A  118  ASP A  130  1                                  13    
HELIX    7 AA7 TYR A  139  THR A  147  1                                   9    
HELIX    8 AA8 VAL B 1722  ARG B 1733  1                                  12    
SHEET    1 AA1 2 THR A  27  ILE A  28  0                                        
SHEET    2 AA1 2 ILE A  64  ASP A  65 -1  O  ILE A  64   N  ILE A  28           
SHEET    1 AA2 2 TYR A 100  ILE A 101  0                                        
SHEET    2 AA2 2 VAL A 137  ASN A 138 -1  O  VAL A 137   N  ILE A 101           
SSBOND   1 CYS B 1723    CYS B 1723                          1555   2657  2.59  
LINK         OD1 ASP A  21                CA    CA A 202     1555   1555  2.32  
LINK         OD1 ASP A  23                CA    CA A 202     1555   1555  2.33  
LINK         OD1 ASP A  25                CA    CA A 202     1555   1555  2.17  
LINK         O   THR A  27                CA    CA A 202     1555   1555  2.30  
LINK         OE1 GLU A  32                CA    CA A 202     1555   1555  2.55  
LINK         OE2 GLU A  32                CA    CA A 202     1555   1555  2.29  
LINK         OD1 ASP A  57                CA    CA A 203     1555   1555  2.25  
LINK         OD1 ASP A  59                CA    CA A 203     1555   1555  2.45  
LINK         OD1 ASN A  61                CA    CA A 203     1555   1555  2.39  
LINK         O   THR A  63                CA    CA A 203     1555   1555  2.21  
LINK         OE1 GLU A  68                CA    CA A 203     1555   1555  2.44  
LINK         OE2 GLU A  68                CA    CA A 203     1555   1555  2.31  
LINK         OD1 ASP A  94                CA    CA A 204     1555   1555  2.33  
LINK         OD1 ASP A  96                CA    CA A 204     1555   1555  2.31  
LINK         OD1 ASN A  98                CA    CA A 204     1555   1555  2.05  
LINK         O   TYR A 100                CA    CA A 204     1555   1555  2.29  
LINK         OE1 GLU A 105                CA    CA A 204     1555   1555  2.25  
LINK         OE2 GLU A 105                CA    CA A 204     1555   1555  2.52  
LINK         OD1 ASP A 130                CA    CA A 201     1555   1555  2.33  
LINK         OD1 ASP A 132                CA    CA A 201     1555   1555  2.41  
LINK         OD1 ASP A 134                CA    CA A 201     1555   1555  2.31  
LINK         O  AGLN A 136                CA    CA A 201     1555   1555  2.23  
LINK         O  BGLN A 136                CA    CA A 201     1555   1555  2.38  
LINK         OE1 GLU A 141                CA    CA A 201     1555   1555  2.33  
LINK         OE2 GLU A 141                CA    CA A 201     1555   1555  2.60  
LINK        CA    CA A 201                 O   HOH A 326     1555   1555  2.43  
LINK        CA    CA A 202                 O   HOH A 338     1555   1555  2.33  
LINK        CA    CA A 203                 O   HOH A 308     1555   1555  2.19  
LINK        CA    CA A 204                 O   HOH A 329     1555   1555  2.48  
SITE     1 AC1  6 ASP A 130  ASP A 132  ASP A 134  GLN A 136                    
SITE     2 AC1  6 GLU A 141  HOH A 326                                          
SITE     1 AC2  6 ASP A  21  ASP A  23  ASP A  25  THR A  27                    
SITE     2 AC2  6 GLU A  32  HOH A 338                                          
SITE     1 AC3  6 ASP A  57  ASP A  59  ASN A  61  THR A  63                    
SITE     2 AC3  6 GLU A  68  HOH A 308                                          
SITE     1 AC4  6 ASP A  94  ASP A  96  ASN A  98  TYR A 100                    
SITE     2 AC4  6 GLU A 105  HOH A 329                                          
CRYST1   58.580   24.433   60.720  90.00 112.63  90.00 P 1 2 1       2          
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      0.017071  0.000000  0.007117        0.00000                         
SCALE2      0.000000  0.040928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017843        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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