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Database: PDB
Entry: 6MUD
LinkDB: 6MUD
Original site: 6MUD 
HEADER    CALCIUM BINDING/TRANSPORT PROTEIN       23-OCT-18   6MUD              
TITLE     VOLTAGE-GATED SODIUM CHANNEL NAV1.5 C-TERMINAL 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 5 SUBUNIT ALPHA;               
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: HH1,SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,    
COMPND   9 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA,VOLTAGE-GATED SODIUM     
COMPND  10 CHANNEL SUBUNIT ALPHA NAV1.5;                                        
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 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SCN5A;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    VOLTAGE-GATED ION CHANNEL, TRANSPORT PROTEIN, EF-HAND DOMAIN, CALCIUM 
KEYWDS   2 BINDING-TRANSPORT PROTEIN COMPLEX                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.GARDILL,C.C.TUNG,F.VAN PETEGEM                                    
REVDAT   5   13-MAR-24 6MUD    1       REMARK                                   
REVDAT   4   08-JAN-20 6MUD    1       REMARK                                   
REVDAT   3   12-JUN-19 6MUD    1       JRNL                                     
REVDAT   2   22-MAY-19 6MUD    1       JRNL                                     
REVDAT   1   08-MAY-19 6MUD    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.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0222                                      
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) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10016                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 459                             
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) : 2.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 601                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 10                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2203                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.54000                                             
REMARK   3    B22 (A**2) : -3.79000                                             
REMARK   3    B33 (A**2) : 6.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.849         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.334         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.519        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2246 ; 0.007 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  1990 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3017 ; 1.055 ; 1.660       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4684 ; 0.813 ; 1.641       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   274 ; 6.089 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;31.882 ;23.478       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   423 ;19.353 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;24.758 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.049 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2535 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   397 ; 0.001 ; 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  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    64                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.932   -6.521  -37.752              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1355 T22:   0.0081                                     
REMARK   3      T33:   0.4552 T12:  -0.0071                                     
REMARK   3      T13:   0.0030 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4134 L22:   2.2341                                     
REMARK   3      L33:   2.0475 L12:  -1.0149                                     
REMARK   3      L13:   2.0029 L23:  -0.9614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2388 S12:  -0.1459 S13:   0.2982                       
REMARK   3      S21:   0.1558 S22:   0.0043 S23:  -0.2223                       
REMARK   3      S31:  -0.0195 S32:  -0.0992 S33:   0.2346                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    65        A   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.552   11.441  -24.863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1982 T22:   0.2013                                     
REMARK   3      T33:   0.4069 T12:  -0.0737                                     
REMARK   3      T13:  -0.0365 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7013 L22:   4.6351                                     
REMARK   3      L33:   2.3536 L12:  -2.6209                                     
REMARK   3      L13:  -1.7283 L23:   1.0259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:  -0.3799 S13:   0.2543                       
REMARK   3      S21:   0.5114 S22:   0.2829 S23:  -0.3079                       
REMARK   3      S31:  -0.0556 S32:   0.0434 S33:  -0.2727                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1785        B  1801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.826   22.420  -61.364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6273 T22:   0.5637                                     
REMARK   3      T33:   0.5132 T12:  -0.2205                                     
REMARK   3      T13:   0.0382 T23:   0.1488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4455 L22:   7.7752                                     
REMARK   3      L33:   4.4793 L12:   1.2657                                     
REMARK   3      L13:   0.0770 L23:  -3.8720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3757 S12:   0.3223 S13:   0.1221                       
REMARK   3      S21:  -0.9804 S22:   0.3194 S23:   0.1037                       
REMARK   3      S31:  -0.0260 S32:   0.3950 S33:   0.0563                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1802        B  1837                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.323   16.905  -51.248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2280 T22:   0.2500                                     
REMARK   3      T33:   0.4305 T12:   0.0065                                     
REMARK   3      T13:   0.0963 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7463 L22:   7.1684                                     
REMARK   3      L33:   3.4803 L12:   2.5132                                     
REMARK   3      L13:  -0.6817 L23:   2.5468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2513 S12:   0.2543 S13:   0.0197                       
REMARK   3      S21:  -0.4969 S22:   0.1744 S23:  -0.4692                       
REMARK   3      S31:   0.0944 S32:   0.6271 S33:   0.0769                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1838        B  1862                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.931   18.067  -50.085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2245 T22:   0.2417                                     
REMARK   3      T33:   0.2925 T12:  -0.0134                                     
REMARK   3      T13:  -0.0007 T23:   0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4497 L22:   9.3894                                     
REMARK   3      L33:   1.0706 L12:   0.6882                                     
REMARK   3      L13:  -0.4129 L23:  -0.1494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1891 S12:   0.1722 S13:   0.0183                       
REMARK   3      S21:  -0.2902 S22:   0.1722 S23:  -0.0773                       
REMARK   3      S31:   0.0435 S32:  -0.1716 S33:   0.0169                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1863        B  1878                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -46.070   28.099  -56.039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1710 T22:   0.3169                                     
REMARK   3      T33:   0.4344 T12:   0.1054                                     
REMARK   3      T13:  -0.0884 T23:  -0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0433 L22:   9.6717                                     
REMARK   3      L33:   7.9802 L12:   0.3662                                     
REMARK   3      L13:   0.4440 L23:  -0.4784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0578 S12:  -0.0053 S13:   0.0562                       
REMARK   3      S21:  -0.4013 S22:  -0.0242 S23:   0.4986                       
REMARK   3      S31:  -0.7038 S32:  -0.1097 S33:   0.0820                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1887        B  1894                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -45.653    8.156  -49.658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0977 T22:   0.2830                                     
REMARK   3      T33:   0.3651 T12:  -0.0817                                     
REMARK   3      T13:   0.0516 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6292 L22:   6.4448                                     
REMARK   3      L33:   8.7070 L12:   0.6997                                     
REMARK   3      L13:   3.6447 L23:  -0.2780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0793 S12:   0.0913 S13:  -0.0001                       
REMARK   3      S21:   0.0196 S22:   0.2011 S23:   0.4038                       
REMARK   3      S31:  -0.1960 S32:   0.1659 S33:  -0.1218                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1895        B  1920                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.521    5.311  -25.964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2249 T22:   0.1178                                     
REMARK   3      T33:   0.3789 T12:  -0.0373                                     
REMARK   3      T13:  -0.0347 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3336 L22:   3.9651                                     
REMARK   3      L33:  11.5792 L12:  -2.0243                                     
REMARK   3      L13:   3.8948 L23:  -5.7806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0807 S12:   0.0839 S13:   0.1023                       
REMARK   3      S21:  -0.0561 S22:  -0.1919 S23:  -0.2307                       
REMARK   3      S31:   0.4026 S32:   0.1923 S33:   0.1112                       
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 : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6MUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237596.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
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-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033000                           
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : K-B PAIR OF BIMORPH MIRRORS        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 11, 2013              
REMARK 200  DATA SCALING SOFTWARE          : XDS NOVEMBER 11, 2013              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.250                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.39                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.890                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-15 % (W/V) PEG 4000, 0.1 M TRIS, PH    
REMARK 280  9.5, 0.1 M MGCL2, AND 5 % (V/V) ISOPROPANOL, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.78950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       70.34200            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.78950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.34200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.78950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.34200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.78950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.34200            
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: 1660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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     MET A     0                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     SER B  1783                                                      
REMARK 465     ASN B  1784                                                      
REMARK 465     PHE B  1879                                                      
REMARK 465     MET B  1880                                                      
REMARK 465     ALA B  1881                                                      
REMARK 465     ALA B  1882                                                      
REMARK 465     ASN B  1883                                                      
REMARK 465     PRO B  1884                                                      
REMARK 465     SER B  1885                                                      
REMARK 465     LYS B  1886                                                      
REMARK 465     LEU B  1921                                                      
REMARK 465     LYS B  1922                                                      
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    ASP A   2       53.09   -108.53                                   
REMARK 500    LYS A 115      172.17    -54.66                                   
REMARK 500    ASP B1802       59.11   -145.35                                   
REMARK 500    SER B1812        3.93    -64.98                                   
REMARK 500    VAL B1843     -166.33    -75.91                                   
REMARK 500    GLN B1918       33.81    -97.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  90         0.12    SIDE CHAIN                              
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 A1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  77.4                                              
REMARK 620 3 ASP A  24   OD1  82.8  81.8                                        
REMARK 620 4 THR A  26   O    88.1 162.4  86.5                                  
REMARK 620 5 GLU A  31   OE1 123.2 120.3 147.4  76.1                            
REMARK 620 6 GLU A  31   OE2  94.3  73.5 155.1 118.1  51.7                      
REMARK 620 7 HOH A1107   O   157.3 102.5  74.8  87.0  76.9 107.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  72.7                                              
REMARK 620 3 ASN A  60   OD1  93.0  85.0                                        
REMARK 620 4 THR A  62   O    71.5 139.9  79.5                                  
REMARK 620 5 GLU A  67   OE1  95.4 126.3 148.7  74.8                            
REMARK 620 6 GLU A  67   OE2  83.7  76.3 161.1 116.6  50.1                      
REMARK 620 7 HOH A1101   O   152.0  91.1 108.5 128.9  75.7  70.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  82.5                                              
REMARK 620 3 ASN A  97   OD1  84.4  92.7                                        
REMARK 620 4 TYR A  99   O    92.3 170.1  78.3                                  
REMARK 620 5 GLU A 104   OE1  95.6  56.1 148.3 133.2                            
REMARK 620 6 GLU A 104   OE2 108.3 105.5 158.8  84.1  49.6                      
REMARK 620 7 HOH A1103   O   163.3  93.3  79.7  89.3  95.4  88.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD2  81.0                                              
REMARK 620 3 ASP A 133   OD1  79.8  85.5                                        
REMARK 620 4 GLN A 135   O    81.4 158.3  78.8                                  
REMARK 620 5 GLU A 140   OE1 112.9 107.7 162.5  90.8                            
REMARK 620 6 GLU A 140   OE2  86.5  66.7 150.7 124.7  45.9                      
REMARK 620 7 HOH A1106   O   163.2  82.3 100.6 115.2  70.9  85.4                
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 A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1004                 
DBREF  6MUD A    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6MUD B 1786  1922  UNP    Q14524   SCN5A_HUMAN   1786   1922             
SEQADV 6MUD SER B 1783  UNP  Q14524              EXPRESSION TAG                 
SEQADV 6MUD ASN B 1784  UNP  Q14524              EXPRESSION TAG                 
SEQADV 6MUD ALA B 1785  UNP  Q14524              EXPRESSION TAG                 
SEQRES   1 A  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 B  140  SER ASN ALA LEU SER GLU ASP ASP PHE ASP MET PHE TYR          
SEQRES   2 B  140  GLU ILE TRP GLU LYS PHE ASP PRO GLU ALA THR GLN PHE          
SEQRES   3 B  140  ILE GLU TYR SER VAL LEU SER ASP PHE ALA ASP ALA LEU          
SEQRES   4 B  140  SER GLU PRO LEU ARG ILE ALA LYS PRO ASN GLN ILE SER          
SEQRES   5 B  140  LEU ILE ASN MET ASP LEU PRO MET VAL SER GLY ASP ARG          
SEQRES   6 B  140  ILE HIS CYS MET ASP ILE LEU PHE ALA PHE THR LYS ARG          
SEQRES   7 B  140  VAL LEU GLY GLU SER GLY GLU MET ASP ALA LEU LYS ILE          
SEQRES   8 B  140  GLN MET GLU GLU LYS PHE MET ALA ALA ASN PRO SER LYS          
SEQRES   9 B  140  ILE SER TYR GLU PRO ILE THR THR THR LEU ARG ARG LYS          
SEQRES  10 B  140  HIS GLU GLU VAL SER ALA MET VAL ILE GLN ARG ALA PHE          
SEQRES  11 B  140  ARG ARG HIS LEU LEU GLN ARG SER LEU LYS                      
HET     CA  A1001       1                                                       
HET     CA  A1002       1                                                       
HET     CA  A1003       1                                                       
HET     CA  A1004       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *15(H2 O)                                                     
HELIX    1 AA1 THR A    5  ASP A   20  1                                  16    
HELIX    2 AA2 THR A   28  LEU A   39  1                                  12    
HELIX    3 AA3 THR A   44  ASP A   56  1                                  13    
HELIX    4 AA4 PHE A   65  ASP A   80  1                                  16    
HELIX    5 AA5 ASP A   80  ASP A   93  1                                  14    
HELIX    6 AA6 SER A  101  MET A  109  1                                   9    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 ASN A  137  MET A  144  1                                   8    
HELIX    9 AA9 SER B 1787  ASP B 1802  1                                  16    
HELIX   10 AB1 VAL B 1813  LEU B 1821  1                                   9    
HELIX   11 AB2 ASN B 1831  MET B 1838  1                                   8    
HELIX   12 AB3 CYS B 1850  GLY B 1863  1                                  14    
HELIX   13 AB4 SER B 1865  LYS B 1878  1                                  14    
HELIX   14 AB5 THR B 1895  GLN B 1918  1                                  24    
SHEET    1 AA1 2 THR A  26  ILE A  27  0                                        
SHEET    2 AA1 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1 AA2 2 PHE B1808  GLU B1810  0                                        
SHEET    2 AA2 2 ARG B1847  HIS B1849 -1  O  ILE B1848   N  ILE B1809           
SHEET    1 AA3 2 PRO B1841  MET B1842  0                                        
SHEET    2 AA3 2 THR B1893  THR B1894 -1  O  THR B1893   N  MET B1842           
LINK         OD1 ASP A  20                CA    CA A1001     1555   1555  2.41  
LINK         OD1 ASP A  22                CA    CA A1001     1555   1555  2.13  
LINK         OD1 ASP A  24                CA    CA A1001     1555   1555  2.34  
LINK         O   THR A  26                CA    CA A1001     1555   1555  2.25  
LINK         OE1 GLU A  31                CA    CA A1001     1555   1555  2.42  
LINK         OE2 GLU A  31                CA    CA A1001     1555   1555  2.66  
LINK         OD1 ASP A  56                CA    CA A1002     1555   1555  2.21  
LINK         OD1 ASP A  58                CA    CA A1002     1555   1555  2.23  
LINK         OD1 ASN A  60                CA    CA A1002     1555   1555  2.69  
LINK         O   THR A  62                CA    CA A1002     1555   1555  2.42  
LINK         OE1 GLU A  67                CA    CA A1002     1555   1555  2.66  
LINK         OE2 GLU A  67                CA    CA A1002     1555   1555  2.49  
LINK         OD1 ASP A  93                CA    CA A1004     1555   1555  2.23  
LINK         OD1 ASP A  95                CA    CA A1004     1555   1555  2.14  
LINK         OD1 ASN A  97                CA    CA A1004     1555   1555  2.34  
LINK         O   TYR A  99                CA    CA A1004     1555   1555  2.04  
LINK         OE1 GLU A 104                CA    CA A1004     1555   1555  2.81  
LINK         OE2 GLU A 104                CA    CA A1004     1555   1555  2.42  
LINK         OD1 ASP A 129                CA    CA A1003     1555   1555  2.34  
LINK         OD2 ASP A 131                CA    CA A1003     1555   1555  2.15  
LINK         OD1 ASP A 133                CA    CA A1003     1555   1555  2.25  
LINK         O   GLN A 135                CA    CA A1003     1555   1555  2.28  
LINK         OE1 GLU A 140                CA    CA A1003     1555   1555  2.55  
LINK         OE2 GLU A 140                CA    CA A1003     1555   1555  2.98  
LINK        CA    CA A1001                 O   HOH A1107     1555   1555  2.27  
LINK        CA    CA A1002                 O   HOH A1101     1555   1555  2.00  
LINK        CA    CA A1003                 O   HOH A1106     1555   1555  2.19  
LINK        CA    CA A1004                 O   HOH A1103     1555   1555  2.36  
CISPEP   1 GLU B 1823    PRO B 1824          0         8.42                     
CISPEP   2 LYS B 1829    PRO B 1830          0        -2.26                     
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A1107                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A1101                                          
SITE     1 AC3  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC3  6 GLU A 140  HOH A1106                                          
SITE     1 AC4  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC4  6 GLU A 104  HOH A1103                                          
CRYST1   65.579   84.032  140.684  90.00  90.00  90.00 I 2 2 2       8          
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      0.015249  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007108        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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