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Database: PDB
Entry: 4UPU
LinkDB: 4UPU
Original site: 4UPU 
HEADER    TRANSFERASE                             18-JUN-14   4UPU              
TITLE     CRYSTAL STRUCTURE OF IP3 3-K CALMODULIN BINDING REGION IN COMPLEX WITH
TITLE    2 CALMODULIN                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 2-149;                                            
COMPND   5 SYNONYM: CAM;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INOSITOL-TRISPHOSPHATE 3-KINASE A;                         
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: CALMODULIN BINDING REGION, RESIDUES 158-183;               
COMPND  11 SYNONYM: INOSITOL 1\,4\,5-TRISPHOSPHATE 3-KINASE A, IP3 3-KINASE A,  
COMPND  12 IP3K A, INSP 3-KINASE A;                                             
COMPND  13 EC: 2.7.1.127;                                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET14B;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;                            
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PKLSLT                                    
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.FRANCO-ECHEVARRIA,J.I.BANOS-SANZ,B.MONTERROSO,A.ROUND,J.SANZ-       
AUTHOR   2 APARICIO,B.GONZALEZ                                                  
REVDAT   4   10-JAN-24 4UPU    1       REMARK LINK                              
REVDAT   3   22-OCT-14 4UPU    1       JRNL                                     
REVDAT   2   10-SEP-14 4UPU    1       TITLE  MASTER                            
REVDAT   1   20-AUG-14 4UPU    0                                                
JRNL        AUTH   E.FRANCO-ECHEVARRIA,J.I.BANOS-SANZ,B.MONTERROSO,A.ROUND,     
JRNL        AUTH 2 J.SANZ-APARICIO,B.GONZALEZ                                   
JRNL        TITL   A NEW CALMODULIN BINDING MOTIF FOR INOSITOL                  
JRNL        TITL 2 1,4,5-TRISPHOSPHATE 3-KINASE REGULATION.                     
JRNL        REF    BIOCHEM.J.                    V. 463   319 2014              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   25101901                                                     
JRNL        DOI    10.1042/BJ20140757                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 14144                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 752                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.34                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1031                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1305                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.77000                                              
REMARK   3    B22 (A**2) : -11.33000                                            
REMARK   3    B33 (A**2) : 5.56000                                              
REMARK   3    B12 (A**2) : -1.80000                                             
REMARK   3    B13 (A**2) : -18.88000                                            
REMARK   3    B23 (A**2) : -2.03000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.039         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.034         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.581         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1342 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1806 ; 1.451 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 5.608 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    74 ;34.239 ;26.216       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   251 ;17.038 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;16.743 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   199 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1024 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   661 ; 2.104 ; 3.285       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   825 ; 3.286 ; 4.903       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   680 ; 3.478 ; 3.663       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U       
REMARK   3  VALUES REFINED INDIVIDUALLY                                         
REMARK   4                                                                      
REMARK   4 4UPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060902.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : KB FOCUSING MIRRORS                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14994                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.90                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.66                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.060                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VAY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% W/V POLYETHYLENE GLYCOL 4000, 0.2    
REMARK 280  M (NH4)2SO4, 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.0 AND 10 MM       
REMARK 280  SPERMIDINE                                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   Y,X,-Z                                                  
REMARK 290      14555   -Y,-X,-Z                                                
REMARK 290      15555   Y,-X,Z                                                  
REMARK 290      16555   -Y,X,Z                                                  
REMARK 290      17555   X,Z,-Y                                                  
REMARK 290      18555   -X,Z,Y                                                  
REMARK 290      19555   -X,-Z,-Y                                                
REMARK 290      20555   X,-Z,Y                                                  
REMARK 290      21555   Z,Y,-X                                                  
REMARK 290      22555   Z,-Y,X                                                  
REMARK 290      23555   -Z,Y,X                                                  
REMARK 290      24555   -Z,-Y,-X                                                
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      26555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      27555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      28555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      30555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      31555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      32555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      34555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      35555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      36555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290      37555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      38555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290      39555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      40555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      41555   X+1/2,Z+1/2,-Y+1/2                                      
REMARK 290      42555   -X+1/2,Z+1/2,Y+1/2                                      
REMARK 290      43555   -X+1/2,-Z+1/2,-Y+1/2                                    
REMARK 290      44555   X+1/2,-Z+1/2,Y+1/2                                      
REMARK 290      45555   Z+1/2,Y+1/2,-X+1/2                                      
REMARK 290      46555   Z+1/2,-Y+1/2,X+1/2                                      
REMARK 290      47555   -Z+1/2,Y+1/2,X+1/2                                      
REMARK 290      48555   -Z+1/2,-Y+1/2,-X+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       79.74000            
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       79.74000            
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       79.74000            
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       79.74000            
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       79.74000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 48-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 119950 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 165820 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2468.9 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  0.000000  1.000000      159.48000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT1   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3   3  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000  0.000000 -1.000000      159.48000            
REMARK 350   BIOMT3   4  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT1   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   5  1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3   5  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT1   6  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT2   6  0.000000  0.000000 -1.000000      159.48000            
REMARK 350   BIOMT3   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.000000  0.000000  1.000000      159.48000            
REMARK 350   BIOMT3   7  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT1   8  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   8  0.000000 -1.000000  0.000000      318.96000            
REMARK 350   BIOMT3   8  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1   9 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   9  0.000000  0.000000 -1.000000      159.48000            
REMARK 350   BIOMT3   9  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT1  10  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT2  10  0.000000  0.000000  1.000000      159.48000            
REMARK 350   BIOMT3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  12  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT2  12  1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  13  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  13  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  14  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT2  14 -1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  15  0.000000 -1.000000  0.000000      318.96000            
REMARK 350   BIOMT3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  16  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  16  1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  16  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT1  17  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  17  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  17 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  18 -1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  18  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT1  19  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  19  0.000000 -1.000000  0.000000      318.96000            
REMARK 350   BIOMT3  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  20  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT2  20  0.000000  0.000000  1.000000      159.48000            
REMARK 350   BIOMT3  20  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  21  0.000000  1.000000  0.000000     -159.48000            
REMARK 350   BIOMT2  21  0.000000  0.000000 -1.000000      159.48000            
REMARK 350   BIOMT3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  22  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  22  0.000000 -1.000000  0.000000      318.96000            
REMARK 350   BIOMT3  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  23  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT2  23 -1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  24  0.000000 -1.000000  0.000000      159.48000            
REMARK 350   BIOMT2  24  1.000000  0.000000  0.000000      159.48000            
REMARK 350   BIOMT3  24  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CA    CA A1153  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2018  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2019  LIES ON A SPECIAL POSITION.                          
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     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     VAL B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     LYS B   164                                                      
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    VAL B 178      -62.74     73.64                                   
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 A1149  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  21   OD1                                                    
REMARK 620 2 ASP A  23   OD1  76.6                                              
REMARK 620 3 ASP A  25   OD1  83.1  79.5                                        
REMARK 620 4 THR A  27   O    81.3 152.5  81.8                                  
REMARK 620 5 GLU A  32   OE1 110.4 128.2 150.6  75.0                            
REMARK 620 6 GLU A  32   OE2 101.8  77.2 154.2 123.8  51.0                      
REMARK 620 7 HOH A2011   O   162.2  87.2  86.8 111.7  85.3  81.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1150  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   OD1                                                    
REMARK 620 2 ASP A  59   OD1  70.2                                              
REMARK 620 3 ASN A  61   OD1  83.8  72.1                                        
REMARK 620 4 THR A  63   O    80.2 145.3  87.4                                  
REMARK 620 5 GLU A  68   OE1  98.2 122.1 165.6  78.9                            
REMARK 620 6 GLU A  68   OE2  77.4  72.2 143.6 119.1  50.0                      
REMARK 620 7 HOH A2030   O   146.7  78.6  97.8 133.0  88.4  82.3                
REMARK 620 8 HOH A2031   O   148.5 131.0  82.6  70.8  88.5 127.7  63.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1151  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  94   OD1                                                    
REMARK 620 2 ASP A  96   OD1  77.3                                              
REMARK 620 3 ASN A  98   OD1  87.5  78.7                                        
REMARK 620 4 TYR A 100   O    85.2 154.7  82.5                                  
REMARK 620 5 GLU A 105   OE1 110.6 129.1 148.7  74.2                            
REMARK 620 6 GLU A 105   OE2  95.5  77.9 155.0 122.5  51.7                      
REMARK 620 7 HOH A2049   O   166.8  89.5  88.2 106.6  79.1  83.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1153  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 119   OD2                                                    
REMARK 620 2 ASP A 119   OD2  91.2                                              
REMARK 620 3 ASP A 119   OD2  95.1  93.9                                        
REMARK 620 4 HOH A2060   O   165.0 102.9  79.1                                  
REMARK 620 5 HOH A2060   O    75.9 155.0 108.3  92.7                            
REMARK 620 6 HOH A2060   O   100.3  72.8 159.7  88.9  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1152  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 130   OD1                                                    
REMARK 620 2 ASP A 132   OD1  82.6                                              
REMARK 620 3 ASP A 134   OD1  89.7  75.7                                        
REMARK 620 4 GLN A 136   O    88.5 150.6  76.4                                  
REMARK 620 5 GLU A 141   OE1 109.4 127.0 151.0  82.3                            
REMARK 620 6 GLU A 141   OE2  90.6  77.0 152.3 131.3  52.4                      
REMARK 620 7 HOH A2071   O   162.0  80.6  80.0 103.2  86.0  91.8                
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 1149                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1150                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1152                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1153                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1154                
DBREF  4UPU A    2   149  UNP    P62158   CALM_HUMAN       2    149             
DBREF  4UPU B  158   183  UNP    P23677   IP3KA_HUMAN    158    183             
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   26  GLY GLU ASP VAL GLY GLN LYS ASN HIS TRP GLN LYS ILE          
SEQRES   2 B   26  ARG THR MET VAL ASN LEU PRO VAL ILE SER PRO PHE LYS          
HET     CA  A1149       1                                                       
HET     CA  A1150       1                                                       
HET     CA  A1151       1                                                       
HET     CA  A1152       1                                                       
HET     CA  A1153       1                                                       
HET    GOL  A1154       6                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CA    5(CA 2+)                                                     
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *81(H2 O)                                                     
HELIX    1   1 THR A    6  ASP A   21  1                                  16    
HELIX    2   2 THR A   29  LEU A   40  1                                  12    
HELIX    3   3 THR A   45  ASP A   57  1                                  13    
HELIX    4   4 PHE A   66  MET A   77  1                                  12    
HELIX    5   5 SER A   82  ASP A   94  1                                  13    
HELIX    6   6 SER A  102  LEU A  113  1                                  12    
HELIX    7   7 THR A  118  ASP A  130  1                                  13    
HELIX    8   8 TYR A  139  ALA A  148  1                                  10    
HELIX    9   9 ASN B  165  ASN B  175  1                                  11    
SHEET    1  AA 2 THR A  27  ILE A  28  0                                        
SHEET    2  AA 2 ILE A  64  ASP A  65 -1  O  ILE A  64   N  ILE A  28           
SHEET    1  AB 2 TYR A 100  ILE A 101  0                                        
SHEET    2  AB 2 VAL A 137  ASN A 138 -1  O  VAL A 137   N  ILE A 101           
LINK         OD1 ASP A  21                CA    CA A1149     1555   1555  2.27  
LINK         OD1 ASP A  23                CA    CA A1149     1555   1555  2.34  
LINK         OD1 ASP A  25                CA    CA A1149     1555   1555  2.44  
LINK         O   THR A  27                CA    CA A1149     1555   1555  2.26  
LINK         OE1 GLU A  32                CA    CA A1149     1555   1555  2.56  
LINK         OE2 GLU A  32                CA    CA A1149     1555   1555  2.47  
LINK         OD1 ASP A  57                CA    CA A1150     1555   1555  2.32  
LINK         OD1 ASP A  59                CA    CA A1150     1555   1555  2.55  
LINK         OD1 ASN A  61                CA    CA A1150     1555   1555  2.31  
LINK         O   THR A  63                CA    CA A1150     1555   1555  2.48  
LINK         OE1 GLU A  68                CA    CA A1150     1555   1555  2.55  
LINK         OE2 GLU A  68                CA    CA A1150     1555   1555  2.57  
LINK         OD1 ASP A  94                CA    CA A1151     1555   1555  2.18  
LINK         OD1 ASP A  96                CA    CA A1151     1555   1555  2.51  
LINK         OD1 ASN A  98                CA    CA A1151     1555   1555  2.39  
LINK         O   TYR A 100                CA    CA A1151     1555   1555  2.24  
LINK         OE1 GLU A 105                CA    CA A1151     1555   1555  2.52  
LINK         OE2 GLU A 105                CA    CA A1151     1555   1555  2.49  
LINK         OD2 ASP A 119                CA    CA A1153     6566   1555  3.04  
LINK         OD2 ASP A 119                CA    CA A1153    12665   1555  3.09  
LINK         OD2 ASP A 119                CA    CA A1153     1555   1555  2.90  
LINK         OD1 ASP A 130                CA    CA A1152     1555   1555  2.28  
LINK         OD1 ASP A 132                CA    CA A1152     1555   1555  2.40  
LINK         OD1 ASP A 134                CA    CA A1152     1555   1555  2.30  
LINK         O   GLN A 136                CA    CA A1152     1555   1555  2.31  
LINK         OE1 GLU A 141                CA    CA A1152     1555   1555  2.39  
LINK         OE2 GLU A 141                CA    CA A1152     1555   1555  2.49  
LINK        CA    CA A1149                 O   HOH A2011     1555   1555  2.23  
LINK        CA    CA A1150                 O   HOH A2030     1555   1555  2.50  
LINK        CA    CA A1150                 O   HOH A2031     1555   1555  2.35  
LINK        CA    CA A1151                 O   HOH A2049     1555   1555  2.45  
LINK        CA    CA A1152                 O   HOH A2071     1555   1555  2.45  
LINK        CA    CA A1153                 O   HOH A2060     1555   1555  2.31  
LINK        CA    CA A1153                 O   HOH A2060     1555   6566  2.33  
LINK        CA    CA A1153                 O   HOH A2060     1555  12665  2.49  
SITE     1 AC1  6 ASP A  21  ASP A  23  ASP A  25  THR A  27                    
SITE     2 AC1  6 GLU A  32  HOH A2011                                          
SITE     1 AC2  7 ASP A  57  ASP A  59  ASN A  61  THR A  63                    
SITE     2 AC2  7 GLU A  68  HOH A2030  HOH A2031                               
SITE     1 AC3  6 ASP A  94  ASP A  96  ASN A  98  TYR A 100                    
SITE     2 AC3  6 GLU A 105  HOH A2049                                          
SITE     1 AC4  6 ASP A 130  ASP A 132  ASP A 134  GLN A 136                    
SITE     2 AC4  6 GLU A 141  HOH A2071                                          
SITE     1 AC5  2 ASP A 119  HOH A2060                                          
SITE     1 AC6  7 SER A 102  GLU A 105  HIS A 108  HOH A2049                    
SITE     2 AC6  7 HOH A2052  HOH A2055  HOH A2074                               
CRYST1  159.480  159.480  159.480  90.00  90.00  90.00 I 4 3 2      48          
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      0.006270  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006270  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006270        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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