GenomeNet

Database: PDB
Entry: 6DAF
LinkDB: 6DAF
Original site: 6DAF 
HEADER    CALCIUM BINDING PROTEIN/MEMBRANE PROTEIN01-MAY-18   6DAF              
TITLE     2.4 ANGSTROM CRYSTAL STRUCTURE OF THE F141L CA/CAM:CAV1.2 IQ DOMAIN   
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN-1;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C; 
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 1611-1644;                                    
COMPND  10 SYNONYM: CALCIUM CHANNEL, L TYPE, ALPHA-1 POLYPEPTIDE, ISOFORM 1,    
COMPND  11 CARDIAC MUSCLE, VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV1.2;  
COMPND  12 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: CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1;                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CALMODULIN, MUTANT, COMPLEX, CALCIUM BINDING PROTEIN-MEMBRANE PROTEIN 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.WANG,F.VAN PETEGEM                                                  
REVDAT   4   17-APR-19 6DAF    1       REMARK                                   
REVDAT   3   21-NOV-18 6DAF    1       JRNL                                     
REVDAT   2   31-OCT-18 6DAF    1       JRNL                                     
REVDAT   1   17-OCT-18 6DAF    0                                                
JRNL        AUTH   K.WANG,C.HOLT,J.LU,M.BROHUS,K.T.LARSEN,M.T.OVERGAARD,        
JRNL        AUTH 2 R.WIMMER,F.VAN PETEGEM                                       
JRNL        TITL   ARRHYTHMIA MUTATIONS IN CALMODULIN CAUSE CONFORMATIONAL      
JRNL        TITL 2 CHANGES THAT AFFECT INTERACTIONS WITH THE CARDIAC            
JRNL        TITL 3 VOLTAGE-GATED CALCIUM CHANNEL.                               
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115 10556 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30348784                                                     
JRNL        DOI    10.1073/PNAS.1808733115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39391                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1974                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.6849 -  5.7812    0.98     2637   140  0.1931 0.2151        
REMARK   3     2  5.7812 -  4.5903    0.99     2709   142  0.1957 0.2277        
REMARK   3     3  4.5903 -  4.0105    0.99     2662   141  0.1641 0.2032        
REMARK   3     4  4.0105 -  3.6440    0.99     2647   136  0.1850 0.2112        
REMARK   3     5  3.6440 -  3.3830    0.99     2645   140  0.2125 0.2837        
REMARK   3     6  3.3830 -  3.1836    0.99     2663   142  0.2172 0.2487        
REMARK   3     7  3.1836 -  3.0242    1.00     2723   144  0.2387 0.3316        
REMARK   3     8  3.0242 -  2.8925    0.99     2641   133  0.2263 0.2776        
REMARK   3     9  2.8925 -  2.7812    0.99     2676   145  0.2295 0.2235        
REMARK   3    10  2.7812 -  2.6853    1.00     2690   141  0.2272 0.2666        
REMARK   3    11  2.6853 -  2.6013    1.00     2714   148  0.2397 0.3094        
REMARK   3    12  2.6013 -  2.5270    1.00     2675   140  0.2462 0.3334        
REMARK   3    13  2.5270 -  2.4604    1.00     2659   137  0.2615 0.3507        
REMARK   3    14  2.4604 -  2.4004    0.97     2676   145  0.2908 0.3416        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 3 THROUGH 78 ) OR (RESID 501     
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2593  11.5154  37.0140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7261 T22:   0.8056                                     
REMARK   3      T33:   0.7215 T12:  -0.0605                                     
REMARK   3      T13:  -0.0609 T23:   0.3109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0932 L22:   3.9637                                     
REMARK   3      L33:   8.4610 L12:   1.2906                                     
REMARK   3      L13:  -0.0448 L23:  -0.6271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0611 S12:   0.0620 S13:   0.3532                       
REMARK   3      S21:   0.4994 S22:  -0.3471 S23:  -0.6151                       
REMARK   3      S31:  -0.9983 S32:   0.9838 S33:   0.2135                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 79 THROUGH 146 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4887  14.9464  16.3527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5763 T22:   0.5407                                     
REMARK   3      T33:   0.4513 T12:   0.0684                                     
REMARK   3      T13:   0.0103 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2189 L22:   9.1986                                     
REMARK   3      L33:   7.0234 L12:  -1.7239                                     
REMARK   3      L13:  -1.0691 L23:  -2.8598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1859 S12:  -0.3837 S13:  -0.6569                       
REMARK   3      S21:   0.4488 S22:  -0.1298 S23:  -0.0675                       
REMARK   3      S31:   0.3132 S32:  -0.3340 S33:   0.3598                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1616 THROUGH 1634 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2564   8.1245  24.8508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8317 T22:   0.8557                                     
REMARK   3      T33:   0.7825 T12:   0.0100                                     
REMARK   3      T13:   0.1300 T23:   0.3604                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9810 L22:   4.6757                                     
REMARK   3      L33:   2.6672 L12:  -0.4373                                     
REMARK   3      L13:  -2.2381 L23:   0.2901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6254 S12:  -0.1905 S13:  -0.4100                       
REMARK   3      S21:   0.1565 S22:   0.1048 S23:   0.1136                       
REMARK   3      S31:   1.4016 S32:  -0.3810 S33:   0.4568                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 3 THROUGH 78 ) OR (RESID 501     
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4461   1.2889  -9.8747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6344 T22:   0.7212                                     
REMARK   3      T33:   0.7317 T12:   0.1809                                     
REMARK   3      T13:  -0.0818 T23:  -0.2737                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5631 L22:   8.2167                                     
REMARK   3      L33:   9.1945 L12:   0.2615                                     
REMARK   3      L13:   1.3051 L23:   4.5237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:  -0.5688 S13:  -0.0927                       
REMARK   3      S21:   0.9122 S22:   0.3925 S23:  -0.7393                       
REMARK   3      S31:   0.8235 S32:   0.8258 S33:  -0.3422                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 79 THROUGH 146 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6357  20.8748  -2.9053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4230 T22:   0.3889                                     
REMARK   3      T33:   0.3764 T12:   0.0722                                     
REMARK   3      T13:  -0.0247 T23:  -0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3264 L22:   7.5458                                     
REMARK   3      L33:   9.6272 L12:   4.4286                                     
REMARK   3      L13:  -4.8173 L23:  -0.9133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0936 S12:   0.5280 S13:  -0.2759                       
REMARK   3      S21:   0.0260 S22:   0.1441 S23:  -0.2163                       
REMARK   3      S31:  -0.4911 S32:  -0.6099 S33:  -0.0550                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1615 THROUGH 1637 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8065  14.6494 -11.6103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5040 T22:   0.6345                                     
REMARK   3      T33:   0.5356 T12:   0.0423                                     
REMARK   3      T13:  -0.0954 T23:  -0.2412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6087 L22:   9.3978                                     
REMARK   3      L33:   6.6999 L12:  -0.8464                                     
REMARK   3      L13:   0.9325 L23:  -3.1455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1523 S12:   0.7544 S13:  -0.0000                       
REMARK   3      S21:  -0.9074 S22:  -0.0404 S23:   0.7133                       
REMARK   3      S31:   0.1040 S32:  -0.5654 S33:   0.1268                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234237.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39395                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.678                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.090                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.430                              
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: PDB ENTRY 2BE6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M POTASSIUM NITRATE, 20% PEG3350,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       17.17750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.94850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.65450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.94850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.17750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.65450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8260 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8290 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     SER C  1608                                                      
REMARK 465     ASN C  1609                                                      
REMARK 465     ALA C  1610                                                      
REMARK 465     ASP C  1611                                                      
REMARK 465     GLU C  1612                                                      
REMARK 465     VAL C  1613                                                      
REMARK 465     THR C  1614                                                      
REMARK 465     VAL C  1615                                                      
REMARK 465     LYS C  1635                                                      
REMARK 465     GLU C  1636                                                      
REMARK 465     GLN C  1637                                                      
REMARK 465     GLY C  1638                                                      
REMARK 465     LEU C  1639                                                      
REMARK 465     VAL C  1640                                                      
REMARK 465     GLY C  1641                                                      
REMARK 465     LYS C  1642                                                      
REMARK 465     PRO C  1643                                                      
REMARK 465     SER C  1644                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ALA B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     SER D  1608                                                      
REMARK 465     ASN D  1609                                                      
REMARK 465     ALA D  1610                                                      
REMARK 465     ASP D  1611                                                      
REMARK 465     GLU D  1612                                                      
REMARK 465     VAL D  1613                                                      
REMARK 465     THR D  1614                                                      
REMARK 465     GLY D  1638                                                      
REMARK 465     LEU D  1639                                                      
REMARK 465     VAL D  1640                                                      
REMARK 465     GLY D  1641                                                      
REMARK 465     LYS D  1642                                                      
REMARK 465     PRO D  1643                                                      
REMARK 465     SER D  1644                                                      
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   6    CG   CD   OE1  OE2                                  
REMARK 470     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     PHE A  19    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     THR A  44    OG1  CG2                                            
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     MET A  51    CG   SD   CE                                        
REMARK 470     ASN A  53    CG   OD1  ND2                                       
REMARK 470     GLU A  54    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     SER A  81    OG                                                  
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     MET A 109    CG   SD   CE                                        
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 123    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 143    CG   CD   OE1  NE2                                  
REMARK 470     LYS C1617    CG   CD   CE   NZ                                   
REMARK 470     GLU C1626    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1630    CG   CD   CE   NZ                                   
REMARK 470     LYS C1633    CG   CD   CE   NZ                                   
REMARK 470     ARG C1634    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B   6    CG   CD   OE1  OE2                                  
REMARK 470     GLU B   7    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     THR B  28    OG1  CG2                                            
REMARK 470     LYS B  30    CG   CD   CE   NZ                                   
REMARK 470     ASN B  42    CG   OD1  ND2                                       
REMARK 470     GLU B  45    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  47    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  49    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  50    CG   OD1  OD2                                       
REMARK 470     VAL B  55    CG1  CG2                                            
REMARK 470     LYS B  77    CG   CD   CE   NZ                                   
REMARK 470     ASP B  78    CG   OD1  OD2                                       
REMARK 470     THR B  79    OG1  CG2                                            
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     LYS D1630    CG   CD   CE   NZ                                   
REMARK 470     LYS D1633    CG   CD   CE   NZ                                   
REMARK 470     ARG D1634    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1635    CG   CD   CE   NZ                                   
REMARK 470     GLU D1636    CG   CD   OE1  OE2                                  
REMARK 470     GLN D1637    CG   CD   OE1  NE2                                  
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    ASN A  42       67.21   -159.95                                   
REMARK 500    ASP A  78      -60.51    -97.38                                   
REMARK 500    LYS A 115       65.34   -118.62                                   
REMARK 500    ASP B  24        8.86    -68.16                                   
REMARK 500    ASN B  42       71.10   -119.28                                   
REMARK 500    ASP B  56       95.34    -63.62                                   
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 A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD2                                                    
REMARK 620 2 ASP A  22   OD1  68.5                                              
REMARK 620 3 ASP A  22   OD2 114.7  47.6                                        
REMARK 620 4 ASP A  24   OD1  75.8  71.9  93.9                                  
REMARK 620 5 THR A  26   O    75.4 137.5 165.6  78.2                            
REMARK 620 6 GLU A  31   OE1  97.5 129.5 111.3 154.2  76.0                      
REMARK 620 7 GLU A  31   OE2  92.4  80.7  68.2 152.5 123.4  50.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  60.3                                              
REMARK 620 3 ASN A  60   OD1  86.0  80.4                                        
REMARK 620 4 THR A  62   O    71.6 130.0  83.4                                  
REMARK 620 5 GLU A  67   OE1  93.8 117.2 159.4  77.0                            
REMARK 620 6 GLU A  67   OE2  68.5  68.6 146.7 107.0  48.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  77.6                                              
REMARK 620 3 ASN A  97   OD1  87.2  76.0                                        
REMARK 620 4 TYR A  99   O    85.0 153.1  82.9                                  
REMARK 620 5 GLU A 104   OE1 107.7 134.2 147.9  70.7                            
REMARK 620 6 GLU A 104   OE2 102.2  81.5 153.1 122.6  52.7                      
REMARK 620 7 HOH A 608   O   165.5  88.2  86.5 107.1  84.3  78.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  72.9                                              
REMARK 620 3 ASP A 133   OD1  82.6  86.6                                        
REMARK 620 4 GLN A 135   O    82.7 152.0  76.6                                  
REMARK 620 5 GLU A 140   OE1 108.8 116.5 156.2  84.0                            
REMARK 620 6 GLU A 140   OE2  88.9  66.6 153.2 127.6  50.3                      
REMARK 620 7 HOH A 601   O   161.3  97.1  81.0 102.2  89.8 101.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  20   OD1                                                    
REMARK 620 2 ASP B  22   OD1  70.5                                              
REMARK 620 3 ASP B  24   OD1  78.8  76.0                                        
REMARK 620 4 THR B  26   O    78.9 148.0  89.5                                  
REMARK 620 5 GLU B  31   OE1 116.2 114.8 163.4  86.6                            
REMARK 620 6 GLU B  31   OE2  93.1  68.7 144.4 123.2  46.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  56   OD1                                                    
REMARK 620 2 ASP B  58   OD1  56.6                                              
REMARK 620 3 ASN B  60   OD1  75.2  64.8                                        
REMARK 620 4 THR B  62   O    70.3 126.4  97.5                                  
REMARK 620 5 GLU B  67   OE1  69.7  56.8 121.4 112.2                            
REMARK 620 6 GLU B  67   OE2  95.4 107.4 170.1  82.1  50.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD1                                                    
REMARK 620 2 ASP B  95   OD1  80.7                                              
REMARK 620 3 ASN B  97   OD1  84.9  73.7                                        
REMARK 620 4 TYR B  99   O    86.3 154.8  83.8                                  
REMARK 620 5 GLU B 104   OE1 107.9 127.6 155.9  76.9                            
REMARK 620 6 GLU B 104   OE2 100.6  77.0 148.9 126.9  50.6                      
REMARK 620 7 HOH B 608   O   173.1  93.3  90.3  98.1  78.4  81.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 129   OD1                                                    
REMARK 620 2 ASP B 131   OD1  75.4                                              
REMARK 620 3 ASP B 133   OD1  80.7  78.2                                        
REMARK 620 4 GLN B 135   O    89.7 149.8  73.4                                  
REMARK 620 5 GLU B 140   OE1  91.7  76.9 155.1 130.5                            
REMARK 620 6 GLU B 140   OE2 110.4 130.0 150.9  79.7  53.8                      
REMARK 620 7 HOH B 606   O   161.3  87.3  89.0 102.3  91.2  86.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 504                  
DBREF  6DAF A    1   148  UNP    P0DP23   CALM1_HUMAN      2    149             
DBREF  6DAF C 1611  1644  UNP    Q13936   CAC1C_HUMAN   1611   1644             
DBREF  6DAF B    1   148  UNP    P0DP23   CALM1_HUMAN      2    149             
DBREF  6DAF D 1611  1644  UNP    Q13936   CAC1C_HUMAN   1611   1644             
SEQADV 6DAF LEU A  141  UNP  P0DP23    PHE   142 ENGINEERED MUTATION            
SEQADV 6DAF SER C 1608  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAF ASN C 1609  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAF ALA C 1610  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAF LEU B  141  UNP  P0DP23    PHE   142 ENGINEERED MUTATION            
SEQADV 6DAF SER D 1608  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAF ASN D 1609  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAF ALA D 1610  UNP  Q13936              EXPRESSION TAG                 
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU LEU VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 C   37  SER ASN ALA ASP GLU VAL THR VAL GLY LYS PHE TYR ALA          
SEQRES   2 C   37  THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS          
SEQRES   3 C   37  ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER                  
SEQRES   1 B  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 B  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 B  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 B  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 B  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 B  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 B  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 B  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 B  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 B  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 B  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU LEU VAL GLN          
SEQRES  12 B  148  MET MET THR ALA LYS                                          
SEQRES   1 D   37  SER ASN ALA ASP GLU VAL THR VAL GLY LYS PHE TYR ALA          
SEQRES   2 D   37  THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS          
SEQRES   3 D   37  ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER                  
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     CA  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HET     CA  B 504       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    8(CA 2+)                                                     
FORMUL  13  HOH   *19(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  THR A   79  1                                  15    
HELIX    5 AA5 ASP A   80  ASP A   93  1                                  14    
HELIX    6 AA6 SER A  101  LEU A  112  1                                  12    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 ASN A  137  THR A  146  1                                  10    
HELIX    9 AA9 LYS C 1617  ARG C 1634  1                                  18    
HELIX   10 AB1 THR B    5  ASP B   20  1                                  16    
HELIX   11 AB2 THR B   28  LEU B   39  1                                  12    
HELIX   12 AB3 THR B   44  ASP B   56  1                                  13    
HELIX   13 AB4 PHE B   65  THR B   79  1                                  15    
HELIX   14 AB5 ASP B   80  ASP B   93  1                                  14    
HELIX   15 AB6 SER B  101  LEU B  112  1                                  12    
HELIX   16 AB7 THR B  117  ASP B  129  1                                  13    
HELIX   17 AB8 ASN B  137  THR B  146  1                                  10    
HELIX   18 AB9 GLY D 1616  LYS D 1635  1                                  20    
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 THR B  26  ILE B  27  0                                        
SHEET    2 AA2 2 ILE B  63  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
LINK         OD2 ASP A  20                CA    CA A 501     1555   1555  2.26  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.33  
LINK         OD2 ASP A  22                CA    CA A 501     1555   1555  2.91  
LINK         OD1 ASP A  24                CA    CA A 501     1555   1555  2.52  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.33  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.44  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.69  
LINK         OD1 ASP A  56                CA    CA A 502     1555   1555  2.82  
LINK         OD1 ASP A  58                CA    CA A 502     1555   1555  2.73  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.35  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.36  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.74  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.56  
LINK         OD1 ASP A  93                CA    CA A 503     1555   1555  2.33  
LINK         OD1 ASP A  95                CA    CA A 503     1555   1555  2.46  
LINK         OD1 ASN A  97                CA    CA A 503     1555   1555  2.30  
LINK         O   TYR A  99                CA    CA A 503     1555   1555  2.30  
LINK         OE1 GLU A 104                CA    CA A 503     1555   1555  2.65  
LINK         OE2 GLU A 104                CA    CA A 503     1555   1555  2.31  
LINK         OD1 ASP A 129                CA    CA A 504     1555   1555  2.39  
LINK         OD1 ASP A 131                CA    CA A 504     1555   1555  2.26  
LINK         OD1 ASP A 133                CA    CA A 504     1555   1555  2.42  
LINK         O   GLN A 135                CA    CA A 504     1555   1555  2.34  
LINK         OE1 GLU A 140                CA    CA A 504     1555   1555  2.46  
LINK         OE2 GLU A 140                CA    CA A 504     1555   1555  2.66  
LINK         OD1 ASP B  20                CA    CA B 501     1555   1555  2.45  
LINK         OD1 ASP B  22                CA    CA B 501     1555   1555  2.25  
LINK         OD1 ASP B  24                CA    CA B 501     1555   1555  2.41  
LINK         O   THR B  26                CA    CA B 501     1555   1555  2.10  
LINK         OE1 GLU B  31                CA    CA B 501     1555   1555  2.21  
LINK         OE2 GLU B  31                CA    CA B 501     1555   1555  2.99  
LINK         OD1 ASP B  56                CA    CA B 502     1555   1555  2.86  
LINK         OD1 ASP B  58                CA    CA B 502     1555   1555  2.93  
LINK         OD1 ASN B  60                CA    CA B 502     1555   1555  2.20  
LINK         O   THR B  62                CA    CA B 502     1555   1555  2.36  
LINK         OE1 GLU B  67                CA    CA B 502     1555   1555  2.64  
LINK         OE2 GLU B  67                CA    CA B 502     1555   1555  2.47  
LINK         OD1 ASP B  93                CA    CA B 503     1555   1555  2.37  
LINK         OD1 ASP B  95                CA    CA B 503     1555   1555  2.40  
LINK         OD1 ASN B  97                CA    CA B 503     1555   1555  2.43  
LINK         O   TYR B  99                CA    CA B 503     1555   1555  2.23  
LINK         OE1 GLU B 104                CA    CA B 503     1555   1555  2.62  
LINK         OE2 GLU B 104                CA    CA B 503     1555   1555  2.53  
LINK         OD1 ASP B 129                CA    CA B 504     1555   1555  2.44  
LINK         OD1 ASP B 131                CA    CA B 504     1555   1555  2.46  
LINK         OD1 ASP B 133                CA    CA B 504     1555   1555  2.38  
LINK         O   GLN B 135                CA    CA B 504     1555   1555  2.31  
LINK         OE1 GLU B 140                CA    CA B 504     1555   1555  2.33  
LINK         OE2 GLU B 140                CA    CA B 504     1555   1555  2.45  
LINK        CA    CA A 503                 O   HOH A 608     1555   1555  2.44  
LINK        CA    CA A 504                 O   HOH A 601     1555   1555  2.47  
LINK        CA    CA B 503                 O   HOH B 608     1555   1555  2.36  
LINK        CA    CA B 504                 O   HOH B 606     1555   1555  2.55  
SITE     1 AC1  5 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  5 GLU A  31                                                     
SITE     1 AC2  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  5 GLU A  67                                                     
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 608                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 601                                          
SITE     1 AC5  5 ASP B  20  ASP B  22  ASP B  24  THR B  26                    
SITE     2 AC5  5 GLU B  31                                                     
SITE     1 AC6  5 ASP B  56  ASP B  58  ASN B  60  THR B  62                    
SITE     2 AC6  5 GLU B  67                                                     
SITE     1 AC7  6 ASP B  93  ASP B  95  ASN B  97  TYR B  99                    
SITE     2 AC7  6 GLU B 104  HOH B 608                                          
SITE     1 AC8  6 ASP B 129  ASP B 131  ASP B 133  GLN B 135                    
SITE     2 AC8  6 GLU B 140  HOH B 606                                          
CRYST1   34.355  121.309  125.897  90.00  90.00  90.00 P 21 21 21    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      0.029108  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008243  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007943        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system