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Database: PDB
Entry: 6DAE
LinkDB: 6DAE
Original site: 6DAE 
HEADER    CALCIUM BINDING PROTEIN/MEMBRANE PROTEIN01-MAY-18   6DAE              
TITLE     2.0 ANGSTROM CRYSTAL STRUCTURE OF THE D95V 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: D, C;                                                         
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,J.LU,F.VAN PETEGEM                                             
REVDAT   4   17-APR-19 6DAE    1       REMARK                                   
REVDAT   3   21-NOV-18 6DAE    1       JRNL                                     
REVDAT   2   31-OCT-18 6DAE    1       JRNL                                     
REVDAT   1   17-OCT-18 6DAE    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.04                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51054                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2555                            
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 43.0489 -  5.2386    1.00     2704   144  0.1718 0.1764        
REMARK   3     2  5.2386 -  4.1591    1.00     2680   138  0.1386 0.2024        
REMARK   3     3  4.1591 -  3.6337    1.00     2706   140  0.1387 0.2016        
REMARK   3     4  3.6337 -  3.3016    1.00     2681   141  0.1784 0.2089        
REMARK   3     5  3.3016 -  3.0650    1.00     2687   141  0.1863 0.2296        
REMARK   3     6  3.0650 -  2.8844    1.00     2723   138  0.1985 0.2478        
REMARK   3     7  2.8844 -  2.7399    1.00     2678   139  0.1977 0.2445        
REMARK   3     8  2.7399 -  2.6207    1.00     2688   144  0.1815 0.2557        
REMARK   3     9  2.6207 -  2.5198    1.00     2667   145  0.1817 0.2346        
REMARK   3    10  2.5198 -  2.4329    1.00     2741   146  0.1730 0.2314        
REMARK   3    11  2.4329 -  2.3568    1.00     2701   142  0.1746 0.2302        
REMARK   3    12  2.3568 -  2.2894    1.00     2684   141  0.1742 0.2029        
REMARK   3    13  2.2894 -  2.2292    1.00     2675   142  0.1914 0.2418        
REMARK   3    14  2.2292 -  2.1748    1.00     2668   143  0.1839 0.2741        
REMARK   3    15  2.1748 -  2.1253    1.00     2734   147  0.1895 0.2681        
REMARK   3    16  2.1253 -  2.0801    1.00     2683   138  0.2111 0.2829        
REMARK   3    17  2.0801 -  2.0385    1.00     2671   143  0.2270 0.2677        
REMARK   3    18  2.0385 -  2.0000    1.00     2728   143  0.2379 0.3127        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.120           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.11                          
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 2 THROUGH 78 ) OR (RESID 501     
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4310   2.1967   0.1329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1185 T22:   0.1319                                     
REMARK   3      T33:   0.1551 T12:   0.0053                                     
REMARK   3      T13:  -0.0064 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6347 L22:   1.5531                                     
REMARK   3      L33:   3.0079 L12:   0.3061                                     
REMARK   3      L13:  -0.9684 L23:   0.2780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:   0.1796 S13:  -0.0183                       
REMARK   3      S21:  -0.0961 S22:  -0.0476 S23:  -0.0332                       
REMARK   3      S31:  -0.0125 S32:  -0.0736 S33:   0.0462                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 79 THROUGH 146 ) OR (RESID       
REMARK   3               504))                                                  
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8246  23.2398  -1.6610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2144 T22:   0.2473                                     
REMARK   3      T33:   0.2119 T12:   0.0726                                     
REMARK   3      T13:   0.0157 T23:   0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6641 L22:   3.1019                                     
REMARK   3      L33:   2.9850 L12:  -0.4930                                     
REMARK   3      L13:   1.0502 L23:   0.9031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0876 S12:   0.2925 S13:   0.2336                       
REMARK   3      S21:  -0.2890 S22:  -0.2370 S23:   0.1062                       
REMARK   3      S31:  -0.3558 S32:  -0.2936 S33:   0.1445                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 3 THROUGH 78) OR (RESID 501      
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8494 -10.1487 -17.6982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.1242                                     
REMARK   3      T33:   0.1446 T12:   0.0012                                     
REMARK   3      T13:   0.0122 T23:   0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4535 L22:   1.5221                                     
REMARK   3      L33:   4.0248 L12:  -0.4677                                     
REMARK   3      L13:  -0.5118 L23:   1.7894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0697 S12:  -0.0455 S13:  -0.0329                       
REMARK   3      S21:  -0.0278 S22:   0.0422 S23:  -0.0493                       
REMARK   3      S31:  -0.0253 S32:  -0.1430 S33:   0.0347                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 79 THROUGH 146 ) OR (RESID       
REMARK   3               504))                                                  
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7140 -19.5707 -17.1639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1729 T22:   0.1493                                     
REMARK   3      T33:   0.1349 T12:   0.0469                                     
REMARK   3      T13:  -0.0041 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2941 L22:   4.2590                                     
REMARK   3      L33:   2.4245 L12:  -0.0590                                     
REMARK   3      L13:   0.0130 L23:  -2.2232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0344 S12:  -0.0163 S13:   0.0080                       
REMARK   3      S21:  -0.0154 S22:  -0.0302 S23:  -0.0987                       
REMARK   3      S31:   0.1311 S32:   0.1650 S33:   0.0682                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1612 THROUGH 1635 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0685 -11.5666 -13.5852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.1556                                     
REMARK   3      T33:   0.1789 T12:   0.0784                                     
REMARK   3      T13:  -0.0091 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8581 L22:   6.0307                                     
REMARK   3      L33:   4.5545 L12:   3.3673                                     
REMARK   3      L13:  -1.0382 L23:   0.4363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0503 S12:  -0.1271 S13:   0.3055                       
REMARK   3      S21:   0.2313 S22:   0.0769 S23:  -0.1628                       
REMARK   3      S31:  -0.2163 S32:   0.1314 S33:  -0.1351                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1612 THROUGH 1634 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3033  14.8819  -4.9423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2321 T22:   0.2346                                     
REMARK   3      T33:   0.2473 T12:   0.0557                                     
REMARK   3      T13:   0.0306 T23:   0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1644 L22:   3.6470                                     
REMARK   3      L33:   3.0447 L12:   4.8333                                     
REMARK   3      L13:  -0.2977 L23:   0.8296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0087 S12:   0.3214 S13:   0.2335                       
REMARK   3      S21:  -0.2368 S22:   0.1179 S23:  -0.1605                       
REMARK   3      S31:  -0.2386 S32:   0.2090 S33:  -0.1203                       
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 6DAE 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_1000234209.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.3                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
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   : 51221                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.039                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.880                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
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         : 2.600                              
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 ENTRIES 2BE6 & 4CDK                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM CHLORIDE, 30% PEG6000,       
REMARK 280  0.1M BICINE, PH 10.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  277K                                                                
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       32.57400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.03900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.80750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.03900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.57400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.80750            
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: 2810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9010 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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: 2780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9100 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
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  1636                                                      
REMARK 465     GLN D  1637                                                      
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 465     SER C  1608                                                      
REMARK 465     ASN C  1609                                                      
REMARK 465     ALA C  1610                                                      
REMARK 465     ASP C  1611                                                      
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 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     ASP A  80    CG   OD1  OD2                                       
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 122    CG   OD1  OD2                                       
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  80    CG   OD1  OD2                                       
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 123    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1612    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1630    CG   CD   CE   NZ                                   
REMARK 470     LYS D1633    CG   CD   CE   NZ                                   
REMARK 470     GLU C1612    CG   CD   OE1  OE2                                  
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 B  56       90.72    -63.85                                   
REMARK 500    ARG D1634       93.50    -67.63                                   
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   OD1                                                    
REMARK 620 2 ASP A  22   OD1  74.0                                              
REMARK 620 3 ASP A  24   OD1  82.0  83.4                                        
REMARK 620 4 THR A  26   O    81.0 152.2  81.3                                  
REMARK 620 5 GLU A  31   OE1  96.8  74.5 157.2 121.2                            
REMARK 620 6 GLU A  31   OE2 117.6 126.4 146.7  76.2  52.9                      
REMARK 620 7 HOH A 650   O   158.7  86.1  88.6 116.5  84.5  80.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  74.2                                              
REMARK 620 3 ASN A  60   OD1  82.9  78.3                                        
REMARK 620 4 THR A  62   O    75.3 144.3  80.0                                  
REMARK 620 5 GLU A  67   OE1  96.9 120.6 160.5  81.0                            
REMARK 620 6 GLU A  67   OE2  83.4  69.7 147.5 124.2  50.9                      
REMARK 620 7 HOH A 618   O   148.3  75.0  98.1 136.3  92.3  79.1                
REMARK 620 8 HOH A 653   O   144.8 130.6  79.8  71.7  89.8 125.7  65.1          
REMARK 620 N                    1     2     3     4     5     6     7           
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 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  80.6                                              
REMARK 620 3 ASP A 133   OD1  79.8  76.7                                        
REMARK 620 4 GLN A 135   O    78.6 150.5  79.2                                  
REMARK 620 5 GLU A 140   OE1 112.5 126.9 153.8  80.9                            
REMARK 620 6 GLU A 140   OE2  98.0  75.3 151.9 128.3  52.5                      
REMARK 620 7 HOH A 664   O   163.8  96.3  84.0  97.8  82.1  96.6                
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  79.3                                              
REMARK 620 3 ASP B  24   OD1  87.4  80.7                                        
REMARK 620 4 THR B  26   O    81.1 156.0  84.6                                  
REMARK 620 5 GLU B  31   OE1  95.4  71.6 151.0 124.3                            
REMARK 620 6 GLU B  31   OE2 110.1 123.6 151.5  76.4  52.5                      
REMARK 620 7 HOH B 634   O   165.8  86.9  87.0 111.3  83.3  80.4                
REMARK 620 N                    1     2     3     4     5     6                 
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  70.3                                              
REMARK 620 3 ASN B  60   OD1  81.7  77.8                                        
REMARK 620 4 THR B  62   O    78.7 144.3  80.5                                  
REMARK 620 5 GLU B  67   OE1  99.1 121.0 160.5  80.6                            
REMARK 620 6 GLU B  67   OE2  81.0  69.3 146.4 123.6  51.7                      
REMARK 620 7 HOH B 608   O   140.0 138.2  80.2  63.3  87.1 129.8                
REMARK 620 8 HOH B 627   O   149.9  79.7  95.2 130.5  93.5  85.8  67.4          
REMARK 620 N                    1     2     3     4     5     6     7           
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 129   OD1                                                    
REMARK 620 2 ASP B 131   OD1  79.5                                              
REMARK 620 3 ASP B 133   OD1  84.8  83.2                                        
REMARK 620 4 GLN B 135   O    82.5 156.1  79.7                                  
REMARK 620 5 GLU B 140   OE1 106.9 121.6 153.7  78.6                            
REMARK 620 6 GLU B 140   OE2  95.5  70.9 153.5 126.6  50.8                      
REMARK 620 7 HOH B 621   O   164.9  94.8  80.7  98.7  88.0  95.8                
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 B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503                  
DBREF  6DAE A    1   148  UNP    P0DP23   CALM1_HUMAN      2    149             
DBREF  6DAE B    1   148  UNP    P0DP23   CALM1_HUMAN      2    149             
DBREF  6DAE D 1611  1644  UNP    Q13936   CAC1C_HUMAN   1611   1644             
DBREF  6DAE C 1611  1644  UNP    Q13936   CAC1C_HUMAN   1611   1644             
SEQADV 6DAE VAL A   95  UNP  P0DP23    ASP    96 ENGINEERED MUTATION            
SEQADV 6DAE VAL B   95  UNP  P0DP23    ASP    96 ENGINEERED MUTATION            
SEQADV 6DAE SER D 1608  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAE ASN D 1609  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAE ALA D 1610  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAE SER C 1608  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAE ASN C 1609  UNP  Q13936              EXPRESSION TAG                 
SEQADV 6DAE ALA C 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 VAL 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 PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
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 VAL 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 PHE 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                  
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                  
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    6(CA 2+)                                                     
FORMUL  11  HOH   *219(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 ALA A  102  GLY A  113  1                                  12    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 TYR A  138  THR A  146  1                                   9    
HELIX    9 AA9 THR B    5  ASP B   20  1                                  16    
HELIX   10 AB1 THR B   28  LEU B   39  1                                  12    
HELIX   11 AB2 THR B   44  ASP B   56  1                                  13    
HELIX   12 AB3 PHE B   65  THR B   79  1                                  15    
HELIX   13 AB4 ASP B   80  ASP B   93  1                                  14    
HELIX   14 AB5 ALA B  102  GLY B  113  1                                  12    
HELIX   15 AB6 THR B  117  ASP B  129  1                                  13    
HELIX   16 AB7 TYR B  138  THR B  146  1                                   9    
HELIX   17 AB8 VAL D 1613  ARG D 1634  1                                  22    
HELIX   18 AB9 VAL C 1613  ARG C 1634  1                                  22    
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 TYR A  99  SER A 101  0                                        
SHEET    2 AA2 2 GLN A 135  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
SHEET    1 AA3 2 THR B  26  ILE B  27  0                                        
SHEET    2 AA3 2 ILE B  63  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
SHEET    1 AA4 2 TYR B  99  SER B 101  0                                        
SHEET    2 AA4 2 GLN B 135  ASN B 137 -1  O  VAL B 136   N  ILE B 100           
LINK         OD1 ASP A  20                CA    CA A 501     1555   1555  2.30  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.36  
LINK         OD1 ASP A  24                CA    CA A 501     1555   1555  2.40  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.33  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.46  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.49  
LINK         OD1 ASP A  56                CA    CA A 502     1555   1555  2.38  
LINK         OD1 ASP A  58                CA    CA A 502     1555   1555  2.42  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.47  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.50  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.53  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.59  
LINK         OD1 ASP A 129                CA    CA A 503     1555   1555  2.32  
LINK         OD1 ASP A 131                CA    CA A 503     1555   1555  2.27  
LINK         OD1 ASP A 133                CA    CA A 503     1555   1555  2.36  
LINK         O   GLN A 135                CA    CA A 503     1555   1555  2.35  
LINK         OE1 GLU A 140                CA    CA A 503     1555   1555  2.46  
LINK         OE2 GLU A 140                CA    CA A 503     1555   1555  2.53  
LINK         OD1 ASP B  20                CA    CA B 501     1555   1555  2.29  
LINK         OD1 ASP B  22                CA    CA B 501     1555   1555  2.27  
LINK         OD1 ASP B  24                CA    CA B 501     1555   1555  2.38  
LINK         O   THR B  26                CA    CA B 501     1555   1555  2.28  
LINK         OE1 GLU B  31                CA    CA B 501     1555   1555  2.48  
LINK         OE2 GLU B  31                CA    CA B 501     1555   1555  2.48  
LINK         OD1 ASP B  56                CA    CA B 502     1555   1555  2.32  
LINK         OD1 ASP B  58                CA    CA B 502     1555   1555  2.45  
LINK         OD1 ASN B  60                CA    CA B 502     1555   1555  2.34  
LINK         O   THR B  62                CA    CA B 502     1555   1555  2.42  
LINK         OE1 GLU B  67                CA    CA B 502     1555   1555  2.47  
LINK         OE2 GLU B  67                CA    CA B 502     1555   1555  2.58  
LINK         OD1 ASP B 129                CA    CA B 503     1555   1555  2.35  
LINK         OD1 ASP B 131                CA    CA B 503     1555   1555  2.38  
LINK         OD1 ASP B 133                CA    CA B 503     1555   1555  2.37  
LINK         O   GLN B 135                CA    CA B 503     1555   1555  2.27  
LINK         OE1 GLU B 140                CA    CA B 503     1555   1555  2.53  
LINK         OE2 GLU B 140                CA    CA B 503     1555   1555  2.58  
LINK        CA    CA A 501                 O   HOH A 650     1555   1555  2.43  
LINK        CA    CA A 502                 O   HOH A 618     1555   1555  2.47  
LINK        CA    CA A 502                 O   HOH A 653     1555   1555  2.45  
LINK        CA    CA A 503                 O   HOH A 664     1555   1555  2.37  
LINK        CA    CA B 501                 O   HOH B 634     1555   1555  2.42  
LINK        CA    CA B 502                 O   HOH B 608     1555   1555  2.54  
LINK        CA    CA B 502                 O   HOH B 627     1555   1555  2.46  
LINK        CA    CA B 503                 O   HOH B 621     1555   1555  2.50  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 650                                          
SITE     1 AC2  7 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  7 GLU A  67  HOH A 618  HOH A 653                               
SITE     1 AC3  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC3  6 GLU A 140  HOH A 664                                          
SITE     1 AC4  6 ASP B  20  ASP B  22  ASP B  24  THR B  26                    
SITE     2 AC4  6 GLU B  31  HOH B 634                                          
SITE     1 AC5  7 ASP B  56  ASP B  58  ASN B  60  THR B  62                    
SITE     2 AC5  7 GLU B  67  HOH B 608  HOH B 627                               
SITE     1 AC6  6 ASP B 129  ASP B 131  ASP B 133  GLN B 135                    
SITE     2 AC6  6 GLU B 140  HOH B 621                                          
CRYST1   65.148   69.615   86.078  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      0.015350  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014365  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011617        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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