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Database: PDB
Entry: 6DAH
LinkDB: 6DAH
Original site: 6DAH 
HEADER    CALCIUM BINDING PROTEIN                 01-MAY-18   6DAH              
TITLE     2.5 ANGSTROM CRYSTAL STRUCTURE OF THE N97S CAM MUTANT                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN-1;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: 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                                         
KEYWDS    CALMODULIN, MUTANT, CALCIUM BINDING PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.WANG,F.VAN PETEGEM                                                  
REVDAT   5   04-OCT-23 6DAH    1       LINK                                     
REVDAT   4   17-APR-19 6DAH    1       REMARK                                   
REVDAT   3   21-NOV-18 6DAH    1       JRNL                                     
REVDAT   2   31-OCT-18 6DAH    1       JRNL                                     
REVDAT   1   17-OCT-18 6DAH    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 43334                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2159                            
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 47.2154 -  6.1653    0.95     2734   145  0.1920 0.1930        
REMARK   3     2  6.1653 -  4.8952    0.94     2709   138  0.2356 0.2625        
REMARK   3     3  4.8952 -  4.2769    0.97     2777   146  0.1753 0.2324        
REMARK   3     4  4.2769 -  3.8861    0.95     2749   140  0.1798 0.2918        
REMARK   3     5  3.8861 -  3.6076    0.97     2789   150  0.1992 0.2701        
REMARK   3     6  3.6076 -  3.3950    0.96     2765   140  0.2243 0.2989        
REMARK   3     7  3.3950 -  3.2250    0.97     2801   150  0.2354 0.3636        
REMARK   3     8  3.2250 -  3.0847    0.94     2702   139  0.2550 0.3609        
REMARK   3     9  3.0847 -  2.9659    0.95     2733   144  0.2622 0.3567        
REMARK   3    10  2.9659 -  2.8636    0.96     2778   144  0.2613 0.3409        
REMARK   3    11  2.8636 -  2.7741    0.96     2739   149  0.2458 0.3047        
REMARK   3    12  2.7741 -  2.6948    0.96     2776   147  0.2539 0.2684        
REMARK   3    13  2.6948 -  2.6238    0.96     2761   147  0.2571 0.3406        
REMARK   3    14  2.6238 -  2.5598    0.95     2726   139  0.2718 0.3093        
REMARK   3    15  2.5598 -  2.5016    0.91     2636   141  0.2839 0.3630        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.81                          
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  : 8                                          
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):  14.5128 -27.4176   3.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2112 T22:   0.2941                                     
REMARK   3      T33:   0.3099 T12:   0.0314                                     
REMARK   3      T13:  -0.0020 T23:   0.0420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0178 L22:   6.4495                                     
REMARK   3      L33:   3.3507 L12:   1.9585                                     
REMARK   3      L13:  -0.0808 L23:   1.7383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0380 S12:  -0.0878 S13:  -0.0504                       
REMARK   3      S21:   0.1184 S22:   0.1989 S23:   0.1730                       
REMARK   3      S31:  -0.0541 S32:   0.2989 S33:  -0.2528                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 79 THROUGH 145 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1597 -28.1799  14.9468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3758 T22:   0.3952                                     
REMARK   3      T33:   0.4928 T12:   0.0627                                     
REMARK   3      T13:  -0.0665 T23:  -0.1241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4652 L22:   3.1540                                     
REMARK   3      L33:   5.7427 L12:  -0.4062                                     
REMARK   3      L13:  -2.9188 L23:   0.5464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0375 S12:  -0.4572 S13:   0.9525                       
REMARK   3      S21:   0.2242 S22:   0.3865 S23:  -0.4634                       
REMARK   3      S31:  -0.1176 S32:   0.2406 S33:  -0.3320                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 12 THROUGH 78 ) OR (RESID 501    
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3493 -19.5735  31.6302              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2901 T22:   0.4129                                     
REMARK   3      T33:   0.3528 T12:   0.0436                                     
REMARK   3      T13:  -0.0037 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0633 L22:   7.8281                                     
REMARK   3      L33:   3.0152 L12:   1.0280                                     
REMARK   3      L13:  -0.9194 L23:   0.3480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0526 S12:  -0.0850 S13:   0.2303                       
REMARK   3      S21:  -0.0047 S22:  -0.0004 S23:  -0.6939                       
REMARK   3      S31:  -0.3600 S32:  -0.2048 S33:  -0.0649                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 79 THROUGH 146 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6542 -22.5511  43.0968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3955 T22:   0.6105                                     
REMARK   3      T33:   0.7296 T12:   0.0692                                     
REMARK   3      T13:   0.0772 T23:   0.0876                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1709 L22:   4.8263                                     
REMARK   3      L33:   4.8899 L12:   0.8132                                     
REMARK   3      L13:  -3.3860 L23:   0.1817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0174 S12:  -0.2107 S13:   1.1187                       
REMARK   3      S21:   0.4592 S22:   0.6037 S23:   1.2041                       
REMARK   3      S31:  -0.0917 S32:  -0.0436 S33:  -0.5753                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND ((RESID -2 THROUGH 78 ) OR (RESID 501    
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.2759   5.8390   4.5662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4439 T22:   0.3746                                     
REMARK   3      T33:   0.6696 T12:   0.0052                                     
REMARK   3      T13:  -0.0227 T23:   0.0625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2840 L22:   1.7818                                     
REMARK   3      L33:   1.7484 L12:  -0.3129                                     
REMARK   3      L13:   1.0141 L23:  -1.4654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1552 S12:  -0.1144 S13:  -0.4365                       
REMARK   3      S21:   0.1168 S22:  -0.3257 S23:  -0.6992                       
REMARK   3      S31:   0.2854 S32:   0.3255 S33:   0.2087                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND ((RESID 79 THROUGH 146 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9945   0.1313  -6.1178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3498 T22:   0.2707                                     
REMARK   3      T33:   0.3925 T12:  -0.0453                                     
REMARK   3      T13:   0.0107 T23:   0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9827 L22:   5.8991                                     
REMARK   3      L33:   4.9125 L12:   1.7692                                     
REMARK   3      L13:  -1.3345 L23:  -2.3507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2150 S12:   0.1787 S13:   0.2419                       
REMARK   3      S21:  -0.4233 S22:   0.2258 S23:   0.6041                       
REMARK   3      S31:   0.4774 S32:  -0.3899 S33:  -0.0386                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'D' AND ((RESID -2 THROUGH 78 ) OR (RESID 501    
REMARK   3               THROUGH 502))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.8185   7.5897  31.1353              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3197 T22:   0.4119                                     
REMARK   3      T33:   0.3428 T12:   0.0594                                     
REMARK   3      T13:  -0.0098 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0351 L22:   3.8577                                     
REMARK   3      L33:   2.4885 L12:  -0.5313                                     
REMARK   3      L13:   1.1683 L23:  -0.0973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0990 S12:   0.2611 S13:  -0.7459                       
REMARK   3      S21:   0.0334 S22:  -0.0392 S23:   0.1176                       
REMARK   3      S31:   0.1172 S32:   0.3204 S33:  -0.0607                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D' AND ((RESID 79 THROUGH 144 ) OR (RESID 503   
REMARK   3               THROUGH 504))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2795   3.9329  20.5369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3649 T22:   0.3863                                     
REMARK   3      T33:   0.3821 T12:  -0.0867                                     
REMARK   3      T13:   0.1076 T23:  -0.1079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5119 L22:   2.5750                                     
REMARK   3      L33:   4.1124 L12:   1.0693                                     
REMARK   3      L13:   2.1077 L23:  -1.7569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0687 S12:  -0.0632 S13:  -0.4886                       
REMARK   3      S21:  -0.1840 S22:   0.2667 S23:  -0.2119                       
REMARK   3      S31:   0.6241 S32:  -0.4903 S33:  -0.1931                       
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 6DAH 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_1000234238.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : 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   : 43340                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.207                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 1.810                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6                               
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 1CLL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1 M BIS-TRIS, PH 6.5,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.20700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     THR A   146                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ALA B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     ALA C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     MET D   145                                                      
REMARK 465     THR D   146                                                      
REMARK 465     ALA D   147                                                      
REMARK 465     LYS D   148                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  14    CG   CD   OE1  OE2                                  
REMARK 470     SER A  17    OG                                                  
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     SER A  38    OG                                                  
REMARK 470     GLN A  41    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
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     GLU A  87    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     LEU A 112    CG   CD1  CD2                                       
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 123    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 143    CG   CD   OE1  NE2                                  
REMARK 470     MET A 144    CG   SD   CE                                        
REMARK 470     MET A 145    CG   SD   CE                                        
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  18    CG   CD1  CD2                                       
REMARK 470     LYS B  30    CG   CD   CE   NZ                                   
REMARK 470     SER B  38    OG                                                  
REMARK 470     LEU B  39    CG   CD1  CD2                                       
REMARK 470     LYS B  77    CG   CD   CE   NZ                                   
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     LEU B 112    CG   CD1  CD2                                       
REMARK 470     GLU B 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     LEU B 116    CG   CD1  CD2                                       
REMARK 470     THR B 117    OG1  CG2                                            
REMARK 470     ASP B 118    CG   OD1  OD2                                       
REMARK 470     GLU B 123    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 130    CG1  CG2  CD1                                       
REMARK 470     ASP B 131    CG   OD1  OD2                                       
REMARK 470     GLN B 135    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 143    CG   CD   OE1  NE2                                  
REMARK 470     GLU C   6    CG   CD   OE1  OE2                                  
REMARK 470     GLU C   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  30    CG   CD   CE   NZ                                   
REMARK 470     ASN C  53    CG   OD1  ND2                                       
REMARK 470     ARG C  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 115    CG   CD   CE   NZ                                   
REMARK 470     GLU C 120    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 123    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 127    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 143    CG   CD   OE1  NE2                                  
REMARK 470     GLU D   7    CG   CD   OE1  OE2                                  
REMARK 470     ILE D   9    CG1  CG2  CD1                                       
REMARK 470     GLU D  11    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  13    CG   CD   CE   NZ                                   
REMARK 470     GLU D  14    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  41    CG   CD   OE1  NE2                                  
REMARK 470     GLN D  49    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  77    CG   CD   CE   NZ                                   
REMARK 470     GLU D  82    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     GLU D 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 115    CG   CD   CE   NZ                                   
REMARK 470     GLU D 123    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 127    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 143    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    GLN A   3       38.37    -85.08                                   
REMARK 500    ASN A  42       85.11   -160.70                                   
REMARK 500    ILE A 130      -20.87   -140.41                                   
REMARK 500    GLN A 143       71.68    -68.92                                   
REMARK 500    ASN B  42       73.87   -151.65                                   
REMARK 500    ASP B  93       73.92    -66.22                                   
REMARK 500    ASP B  95      -72.21    -72.23                                   
REMARK 500    SER B  97        2.82    -63.47                                   
REMARK 500    GLU B 114       10.68    -65.56                                   
REMARK 500    LYS B 115      -79.23    -82.82                                   
REMARK 500    ASP B 118     -159.61   -131.42                                   
REMARK 500    GLU B 120       -2.31    -58.01                                   
REMARK 500    ALA B 128       38.53   -141.50                                   
REMARK 500    ILE B 130      -64.47    -98.80                                   
REMARK 500    MET B 145        6.72    -68.38                                   
REMARK 500    ASP C  93       70.57    -69.84                                   
REMARK 500    ASP D  20       64.86    -69.33                                   
REMARK 500    ASN D  42       75.39   -157.54                                   
REMARK 500    ASP D  93       67.99    -63.35                                   
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  83.8                                              
REMARK 620 3 ASP A  24   OD1  81.4  87.7                                        
REMARK 620 4 THR A  26   O    82.2 163.6  81.7                                  
REMARK 620 5 GLU A  31   OE1 112.6 119.7 149.5  74.0                            
REMARK 620 6 GLU A  31   OE2 106.1  68.6 153.7 123.8  51.2                      
REMARK 620 7 HOH A 604   O   160.2  76.6  94.8 116.7  80.3  69.4                
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  74.6                                              
REMARK 620 3 ASP A  58   OD2 119.5  45.2                                        
REMARK 620 4 ASN A  60   OD1  84.3  71.1  81.4                                  
REMARK 620 5 THR A  62   O    77.4 143.5 155.6  83.3                            
REMARK 620 6 GLU A  67   OE1 114.2 132.7 105.0 151.7  80.4                      
REMARK 620 7 GLU A  67   OE2  86.7  85.3  84.0 156.2 116.1  51.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  82.3                                              
REMARK 620 3 SER A  97   OG   92.5  75.6                                        
REMARK 620 4 TYR A  99   O    78.3 149.7  82.2                                  
REMARK 620 5 GLU A 104   OE1  89.9  69.2 144.0 133.2                            
REMARK 620 6 GLU A 104   OE2  96.8 120.7 162.1  84.8  51.5                      
REMARK 620 N                    1     2     3     4     5                       
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  80.7                                              
REMARK 620 3 ASP A 133   OD1  76.3  80.5                                        
REMARK 620 4 GLN A 135   O    70.3 141.2  68.2                                  
REMARK 620 5 GLU A 140   OE1 100.7 127.8 151.2  83.7                            
REMARK 620 6 GLU A 140   OE2  64.1  80.7 138.3 107.6  55.5                      
REMARK 620 N                    1     2     3     4     5                       
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  69.1                                              
REMARK 620 3 ASP B  22   OD2 112.7  43.6                                        
REMARK 620 4 ASP B  24   OD1  75.8  82.5  93.7                                  
REMARK 620 5 THR B  26   O    74.2 141.4 167.1  77.1                            
REMARK 620 6 GLU B  31   OE1  84.1  77.5  81.3 155.6 110.8                      
REMARK 620 7 GLU B  31   OE2 100.8 128.1 117.4 146.6  70.2  50.5                
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  66.9                                              
REMARK 620 3 ASP B  58   OD2 111.9  47.7                                        
REMARK 620 4 ASN B  60   OD1  89.9  82.1  97.2                                  
REMARK 620 5 THR B  62   O    80.3 139.2 165.3  73.9                            
REMARK 620 6 GLU B  67   OE1  82.0  74.3  66.0 156.4 125.8                      
REMARK 620 7 GLU B  67   OE2 101.5 124.3 100.4 153.6  84.5  50.0                
REMARK 620 N                    1     2     3     4     5     6                 
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  68.9                                              
REMARK 620 3 SER B  97   OG   96.2  94.4                                        
REMARK 620 4 TYR B  99   O    88.1 153.8  75.1                                  
REMARK 620 5 GLU B 104   OE1 101.8 117.5 147.2  78.3                            
REMARK 620 6 GLU B 104   OE2  91.7  64.6 153.0 131.0  53.8                      
REMARK 620 N                    1     2     3     4     5                       
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 133   OD1 107.8                                              
REMARK 620 3 GLN B 135   O   103.8  79.0                                        
REMARK 620 4 GLU B 140   OE1  93.6 146.8  71.3                                  
REMARK 620 5 GLU B 140   OE2  88.4 153.7 117.9  47.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  20   OD1                                                    
REMARK 620 2 ASP C  22   OD1  70.9                                              
REMARK 620 3 ASP C  24   OD1  69.6  71.9                                        
REMARK 620 4 THR C  26   O    83.5 150.0  84.8                                  
REMARK 620 5 GLU C  31   OE1  98.4  72.5 144.5 128.3                            
REMARK 620 6 GLU C  31   OE2 129.5 124.8 155.9  83.6  55.5                      
REMARK 620 7 ASP D 118   OD2  66.9 106.7 133.8  75.9  58.5  62.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  56   OD1                                                    
REMARK 620 2 ASP C  58   OD1  76.4                                              
REMARK 620 3 ASP C  58   OD2 125.9  54.3                                        
REMARK 620 4 ASN C  60   OD1  82.7  64.3  93.5                                  
REMARK 620 5 THR C  62   O    80.8 135.3 149.9  75.1                            
REMARK 620 6 GLU C  67   OE1  90.6  87.6  68.6 151.9 130.9                      
REMARK 620 7 GLU C  67   OE2 111.3 137.3  94.1 155.3  86.8  51.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  93   OD1                                                    
REMARK 620 2 ASP C  95   OD1  87.2                                              
REMARK 620 3 SER C  97   OG   83.5  76.1                                        
REMARK 620 4 TYR C  99   O    86.4 152.7  76.8                                  
REMARK 620 5 GLU C 104   OE1 111.3  71.4 143.1 135.4                            
REMARK 620 6 GLU C 104   OE2 104.6 127.4 154.8  79.9  56.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 129   OD1                                                    
REMARK 620 2 ASP C 131   OD1  72.1                                              
REMARK 620 3 ASP C 133   OD1  84.9  84.1                                        
REMARK 620 4 GLN C 135   O    74.9 142.7  75.9                                  
REMARK 620 5 GLU C 140   OE1 105.9 130.6 145.2  75.3                            
REMARK 620 6 GLU C 140   OE2  94.6  80.3 163.7 119.7  50.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  20   OD1                                                    
REMARK 620 2 ASP D  22   OD1  73.8                                              
REMARK 620 3 ASP D  24   OD1  70.9  82.7                                        
REMARK 620 4 THR D  26   O    71.7 144.1  77.2                                  
REMARK 620 5 GLU D  31   OE1 126.0 129.9 144.5  79.9                            
REMARK 620 6 GLU D  31   OE2 106.6  78.4 160.8 120.8  52.7                      
REMARK 620 7 HOH D 601   O   154.5  85.0  93.0 125.2  78.6  82.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  56   OD1                                                    
REMARK 620 2 ASP D  58   OD1  75.1                                              
REMARK 620 3 ASN D  60   OD1  90.2  85.6                                        
REMARK 620 4 THR D  62   O    85.9 155.8  79.6                                  
REMARK 620 5 GLU D  67   OE1 105.1 125.9 147.3  73.1                            
REMARK 620 6 GLU D  67   OE2  85.2  76.1 161.7 117.7  50.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  93   OD1                                                    
REMARK 620 2 ASP D  95   OD1  85.4                                              
REMARK 620 3 SER D  97   OG   87.2  75.4                                        
REMARK 620 4 TYR D  99   O    82.4 158.3  86.1                                  
REMARK 620 5 GLU D 104   OE1 101.2  72.1 145.5 127.9                            
REMARK 620 6 GLU D 104   OE2 110.7 127.5 150.5  73.8  56.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 129   OD1                                                    
REMARK 620 2 ASP D 131   OD2 102.8                                              
REMARK 620 3 ASP D 133   OD1  70.1 113.1                                        
REMARK 620 4 GLN D 135   O    77.5 179.6  66.7                                  
REMARK 620 5 GLU D 140   OE1  81.0  65.0 150.1 115.4                            
REMARK 620 6 GLU D 140   OE2 101.4 101.9 145.0  78.3  47.8                      
REMARK 620 N                    1     2     3     4     5                       
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                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 504                  
DBREF  6DAH A    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6DAH B    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6DAH C    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6DAH D    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
SEQADV 6DAH GLY A   -2  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH HIS A   -1  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH SER A   97  UNP  P0DP23    ASN    98 ENGINEERED MUTATION            
SEQADV 6DAH GLY B   -2  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH HIS B   -1  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH SER B   97  UNP  P0DP23    ASN    98 ENGINEERED MUTATION            
SEQADV 6DAH GLY C   -2  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH HIS C   -1  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH SER C   97  UNP  P0DP23    ASN    98 ENGINEERED MUTATION            
SEQADV 6DAH GLY D   -2  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH HIS D   -1  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6DAH SER D   97  UNP  P0DP23    ASN    98 ENGINEERED MUTATION            
SEQRES   1 A  151  GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA          
SEQRES   2 A  151  GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY          
SEQRES   3 A  151  ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET          
SEQRES   4 A  151  ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN          
SEQRES   5 A  151  ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR          
SEQRES   6 A  151  ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS          
SEQRES   7 A  151  MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA          
SEQRES   8 A  151  PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER          
SEQRES   9 A  151  ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU          
SEQRES  10 A  151  LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU          
SEQRES  11 A  151  ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU          
SEQRES  12 A  151  PHE VAL GLN MET MET THR ALA LYS                              
SEQRES   1 B  151  GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA          
SEQRES   2 B  151  GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY          
SEQRES   3 B  151  ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET          
SEQRES   4 B  151  ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN          
SEQRES   5 B  151  ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR          
SEQRES   6 B  151  ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS          
SEQRES   7 B  151  MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA          
SEQRES   8 B  151  PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER          
SEQRES   9 B  151  ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU          
SEQRES  10 B  151  LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU          
SEQRES  11 B  151  ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU          
SEQRES  12 B  151  PHE VAL GLN MET MET THR ALA LYS                              
SEQRES   1 C  151  GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA          
SEQRES   2 C  151  GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY          
SEQRES   3 C  151  ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET          
SEQRES   4 C  151  ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN          
SEQRES   5 C  151  ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR          
SEQRES   6 C  151  ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS          
SEQRES   7 C  151  MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA          
SEQRES   8 C  151  PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER          
SEQRES   9 C  151  ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU          
SEQRES  10 C  151  LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU          
SEQRES  11 C  151  ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU          
SEQRES  12 C  151  PHE VAL GLN MET MET THR ALA LYS                              
SEQRES   1 D  151  GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA          
SEQRES   2 D  151  GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY          
SEQRES   3 D  151  ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET          
SEQRES   4 D  151  ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN          
SEQRES   5 D  151  ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR          
SEQRES   6 D  151  ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS          
SEQRES   7 D  151  MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA          
SEQRES   8 D  151  PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER          
SEQRES   9 D  151  ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU          
SEQRES  10 D  151  LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU          
SEQRES  11 D  151  ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU          
SEQRES  12 D  151  PHE VAL GLN MET MET THR ALA LYS                              
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                                                       
HET     CA  C 501       1                                                       
HET     CA  C 502       1                                                       
HET     CA  C 503       1                                                       
HET     CA  C 504       1                                                       
HET     CA  D 501       1                                                       
HET     CA  D 502       1                                                       
HET     CA  D 503       1                                                       
HET     CA  D 504       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    16(CA 2+)                                                    
FORMUL  21  HOH   *34(H2 O)                                                     
HELIX    1 AA1 HIS A   -1  GLN A    3  5                                   5    
HELIX    2 AA2 THR A    5  SER A   17  1                                  13    
HELIX    3 AA3 THR A   28  LEU A   39  1                                  12    
HELIX    4 AA4 THR A   44  GLU A   54  1                                  11    
HELIX    5 AA5 PHE A   65  ASP A   93  1                                  29    
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 TYR A  138  GLN A  143  1                                   6    
HELIX    9 AA9 LYS B   13  ASP B   20  1                                   8    
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  ASP B   93  1                                  29    
HELIX   13 AB4 SER B  101  LEU B  112  1                                  12    
HELIX   14 AB5 GLU B  120  ALA B  128  1                                   9    
HELIX   15 AB6 ASN B  137  MET B  145  1                                   9    
HELIX   16 AB7 HIS C   -1  LEU C    4  5                                   6    
HELIX   17 AB8 THR C    5  ASP C   20  1                                  16    
HELIX   18 AB9 THR C   28  LEU C   39  1                                  12    
HELIX   19 AC1 THR C   44  GLU C   54  1                                  11    
HELIX   20 AC2 ASP C   64  ASP C   93  1                                  30    
HELIX   21 AC3 SER C  101  ASN C  111  1                                  11    
HELIX   22 AC4 THR C  117  ASP C  129  1                                  13    
HELIX   23 AC5 ASN C  137  MET C  145  1                                   9    
HELIX   24 AC6 MET D    0  LEU D    4  5                                   5    
HELIX   25 AC7 THR D    5  ASP D   20  1                                  16    
HELIX   26 AC8 THR D   28  LEU D   39  1                                  12    
HELIX   27 AC9 THR D   44  ASP D   56  1                                  13    
HELIX   28 AD1 PHE D   65  ASP D   93  1                                  29    
HELIX   29 AD2 SER D  101  LEU D  112  1                                  12    
HELIX   30 AD3 THR D  117  ASP D  129  1                                  13    
HELIX   31 AD4 ASN D  137  GLN D  143  1                                   7    
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  ILE A 100  0                                        
SHEET    2 AA2 2 VAL A 136  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 THR D  26  ILE D  27  0                                        
SHEET    2 AA4 2 ILE D  63  ASP D  64 -1  O  ILE D  63   N  ILE D  27           
LINK         OD1 ASP A  20                CA    CA A 501     1555   1555  2.27  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.41  
LINK         OD1 ASP A  24                CA    CA A 501     1555   1555  2.31  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.24  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.69  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.33  
LINK         OD1 ASP A  56                CA    CA A 502     1555   1555  2.29  
LINK         OD1 ASP A  58                CA    CA A 502     1555   1555  2.37  
LINK         OD2 ASP A  58                CA    CA A 502     1555   1555  3.10  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.42  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.41  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.52  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.57  
LINK         OD1 ASP A  93                CA    CA A 503     1555   1555  2.19  
LINK         OD1 ASP A  95                CA    CA A 503     1555   1555  2.18  
LINK         OG  SER A  97                CA    CA A 503     1555   1555  2.60  
LINK         O   TYR A  99                CA    CA A 503     1555   1555  2.20  
LINK         OE1 GLU A 104                CA    CA A 503     1555   1555  2.61  
LINK         OE2 GLU A 104                CA    CA A 503     1555   1555  2.43  
LINK         OD1 ASP A 129                CA    CA A 504     1555   1555  2.51  
LINK         OD1 ASP A 131                CA    CA A 504     1555   1555  2.20  
LINK         OD1 ASP A 133                CA    CA A 504     1555   1555  2.32  
LINK         O   GLN A 135                CA    CA A 504     1555   1555  2.52  
LINK         OE1 GLU A 140                CA    CA A 504     1555   1555  2.23  
LINK         OE2 GLU A 140                CA    CA A 504     1555   1555  2.46  
LINK        CA    CA A 501                 O   HOH A 604     1555   1555  2.82  
LINK         OD1 ASP B  20                CA    CA B 501     1555   1555  2.38  
LINK         OD1 ASP B  22                CA    CA B 501     1555   1555  2.45  
LINK         OD2 ASP B  22                CA    CA B 501     1555   1555  3.17  
LINK         OD1 ASP B  24                CA    CA B 501     1555   1555  2.42  
LINK         O   THR B  26                CA    CA B 501     1555   1555  2.47  
LINK         OE1 GLU B  31                CA    CA B 501     1555   1555  2.72  
LINK         OE2 GLU B  31                CA    CA B 501     1555   1555  2.41  
LINK         OD1 ASP B  56                CA    CA B 502     1555   1555  2.46  
LINK         OD1 ASP B  58                CA    CA B 502     1555   1555  2.45  
LINK         OD2 ASP B  58                CA    CA B 502     1555   1555  2.89  
LINK         OD1 ASN B  60                CA    CA B 502     1555   1555  2.40  
LINK         O   THR B  62                CA    CA B 502     1555   1555  2.42  
LINK         OE1 GLU B  67                CA    CA B 502     1555   1555  2.60  
LINK         OE2 GLU B  67                CA    CA B 502     1555   1555  2.60  
LINK         OD1 ASP B  93                CA    CA B 503     1555   1555  2.24  
LINK         OD1 ASP B  95                CA    CA B 503     1555   1555  2.48  
LINK         OG  SER B  97                CA    CA B 503     1555   1555  2.30  
LINK         O   TYR B  99                CA    CA B 503     1555   1555  2.32  
LINK         OE1 GLU B 104                CA    CA B 503     1555   1555  2.37  
LINK         OE2 GLU B 104                CA    CA B 503     1555   1555  2.48  
LINK         OD1 ASP B 129                CA    CA B 504     1555   1555  2.75  
LINK         OD1 ASP B 133                CA    CA B 504     1555   1555  2.61  
LINK         O   GLN B 135                CA    CA B 504     1555   1555  2.48  
LINK         OE1 GLU B 140                CA    CA B 504     1555   1555  2.94  
LINK         OE2 GLU B 140                CA    CA B 504     1555   1555  2.41  
LINK         OD1 ASP C  20                CA    CA C 501     1555   1555  2.29  
LINK         OD1 ASP C  22                CA    CA C 501     1555   1555  2.71  
LINK         OD1 ASP C  24                CA    CA C 501     1555   1555  2.49  
LINK         O   THR C  26                CA    CA C 501     1555   1555  2.39  
LINK         OE1 GLU C  31                CA    CA C 501     1555   1555  2.36  
LINK         OE2 GLU C  31                CA    CA C 501     1555   1555  2.40  
LINK         OD1 ASP C  56                CA    CA C 502     1555   1555  2.28  
LINK         OD1 ASP C  58                CA    CA C 502     1555   1555  2.39  
LINK         OD2 ASP C  58                CA    CA C 502     1555   1555  2.44  
LINK         OD1 ASN C  60                CA    CA C 502     1555   1555  2.54  
LINK         O   THR C  62                CA    CA C 502     1555   1555  2.46  
LINK         OE1 GLU C  67                CA    CA C 502     1555   1555  2.54  
LINK         OE2 GLU C  67                CA    CA C 502     1555   1555  2.54  
LINK         OD1 ASP C  93                CA    CA C 503     1555   1555  2.43  
LINK         OD1 ASP C  95                CA    CA C 503     1555   1555  2.36  
LINK         OG  SER C  97                CA    CA C 503     1555   1555  2.52  
LINK         O   TYR C  99                CA    CA C 503     1555   1555  2.34  
LINK         OE1 GLU C 104                CA    CA C 503     1555   1555  2.34  
LINK         OE2 GLU C 104                CA    CA C 503     1555   1555  2.36  
LINK         OD1 ASP C 129                CA    CA C 504     1555   1555  2.50  
LINK         OD1 ASP C 131                CA    CA C 504     1555   1555  2.34  
LINK         OD1 ASP C 133                CA    CA C 504     1555   1555  2.44  
LINK         O   GLN C 135                CA    CA C 504     1555   1555  2.44  
LINK         OE1 GLU C 140                CA    CA C 504     1555   1555  2.61  
LINK         OE2 GLU C 140                CA    CA C 504     1555   1555  2.57  
LINK        CA    CA C 501                 OD2 ASP D 118     1455   1555  2.79  
LINK         OD1 ASP D  20                CA    CA D 501     1555   1555  2.33  
LINK         OD1 ASP D  22                CA    CA D 501     1555   1555  2.38  
LINK         OD1 ASP D  24                CA    CA D 501     1555   1555  2.47  
LINK         O   THR D  26                CA    CA D 501     1555   1555  2.48  
LINK         OE1 GLU D  31                CA    CA D 501     1555   1555  2.63  
LINK         OE2 GLU D  31                CA    CA D 501     1555   1555  2.28  
LINK         OD1 ASP D  56                CA    CA D 502     1555   1555  2.29  
LINK         OD1 ASP D  58                CA    CA D 502     1555   1555  2.40  
LINK         OD1 ASN D  60                CA    CA D 502     1555   1555  2.35  
LINK         O   THR D  62                CA    CA D 502     1555   1555  2.34  
LINK         OE1 GLU D  67                CA    CA D 502     1555   1555  2.66  
LINK         OE2 GLU D  67                CA    CA D 502     1555   1555  2.46  
LINK         OD1 ASP D  93                CA    CA D 503     1555   1555  2.25  
LINK         OD1 ASP D  95                CA    CA D 503     1555   1555  2.31  
LINK         OG  SER D  97                CA    CA D 503     1555   1555  2.77  
LINK         O   TYR D  99                CA    CA D 503     1555   1555  2.28  
LINK         OE1 GLU D 104                CA    CA D 503     1555   1555  2.35  
LINK         OE2 GLU D 104                CA    CA D 503     1555   1555  2.30  
LINK         OD1 ASP D 129                CA    CA D 504     1555   1555  2.52  
LINK         OD2 ASP D 131                CA    CA D 504     1555   1555  2.48  
LINK         OD1 ASP D 133                CA    CA D 504     1555   1555  2.28  
LINK         O   GLN D 135                CA    CA D 504     1555   1555  2.79  
LINK         OE1 GLU D 140                CA    CA D 504     1555   1555  2.84  
LINK         OE2 GLU D 140                CA    CA D 504     1555   1555  2.52  
LINK        CA    CA D 501                 O   HOH D 601     1555   1555  2.44  
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 604                                          
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  5 ASP A  93  ASP A  95  SER A  97  TYR A  99                    
SITE     2 AC3  5 GLU A 104                                                     
SITE     1 AC4  5 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  5 GLU A 140                                                     
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  5 ASP B  93  ASP B  95  SER B  97  TYR B  99                    
SITE     2 AC7  5 GLU B 104                                                     
SITE     1 AC8  6 ASP B 129  ASP B 131  GLY B 132  ASP B 133                    
SITE     2 AC8  6 GLN B 135  GLU B 140                                          
SITE     1 AC9  6 ASP C  20  ASP C  22  ASP C  24  THR C  26                    
SITE     2 AC9  6 GLU C  31  ASP D 118                                          
SITE     1 AD1  5 ASP C  56  ASP C  58  ASN C  60  THR C  62                    
SITE     2 AD1  5 GLU C  67                                                     
SITE     1 AD2  5 ASP C  93  ASP C  95  SER C  97  TYR C  99                    
SITE     2 AD2  5 GLU C 104                                                     
SITE     1 AD3  5 ASP C 129  ASP C 131  ASP C 133  GLN C 135                    
SITE     2 AD3  5 GLU C 140                                                     
SITE     1 AD4  6 ASP D  20  ASP D  22  ASP D  24  THR D  26                    
SITE     2 AD4  6 GLU D  31  HOH D 601                                          
SITE     1 AD5  5 ASP D  56  ASP D  58  ASN D  60  THR D  62                    
SITE     2 AD5  5 GLU D  67                                                     
SITE     1 AD6  5 ASP D  93  ASP D  95  SER D  97  TYR D  99                    
SITE     2 AD6  5 GLU D 104                                                     
SITE     1 AD7  5 ASP D 129  ASP D 131  ASP D 133  GLN D 135                    
SITE     2 AD7  5 GLU D 140                                                     
CRYST1   59.117   94.414   60.977  90.00  94.42  90.00 P 1 21 1      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      0.016916  0.000000  0.001308        0.00000                         
SCALE2      0.000000  0.010592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016449        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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