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Database: PDB
Entry: 3BYA
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Original site: 3BYA 
HEADER    METAL BINDING PROTEIN                   15-JAN-08   3BYA              
TITLE     STRUCTURE OF A CALMODULIN COMPLEX                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1 PEPTIDE;          
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: N-METHYL-D-ASPARTATE RECEPTOR SUBUNIT NR1;                  
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB12;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE. THE SEQUENCE IS NATURALLY FOUND IN 
SOURCE  14 HUMAN (HOMO SAPIENS).                                                
KEYWDS    CALMODULIN, EF HAND MOTIF, NR1, N-METHYL-D-ASPARTATE RECEPTOR,        
KEYWDS   2 GLUTAMATE, CENTRAL NERVOUS SYSTEM, NEURONAL CHANNEL, CALCIUM         
KEYWDS   3 CHANNEL, METHYLATION, PHOSPHOPROTEIN, CELL JUNCTION, GLYCOPROTEIN,   
KEYWDS   4 ION TRANSPORT, IONIC CHANNEL, MAGNESIUM, MEMBRANE, POSTSYNAPTIC CELL 
KEYWDS   5 MEMBRANE, SYNAPSE, TRANSMEMBRANE, TRANSPORT, METAL BINDING PROTEIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BIRRANE,A.SONI,J.A.A.LADIAS                                         
REVDAT   3   30-AUG-23 3BYA    1       REMARK                                   
REVDAT   2   13-JUL-11 3BYA    1       VERSN                                    
REVDAT   1   20-JAN-09 3BYA    0                                                
JRNL        AUTH   G.BIRRANE,A.SONI,J.A.A.LADIAS                                
JRNL        TITL   STRUCTURE OF A CALMODULIN COMPLEX                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 13948                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 735                             
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1005                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1239                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.06000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.438         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1288 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   879 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1733 ; 1.682 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2156 ; 0.998 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 5.330 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    70 ;35.591 ;25.857       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   251 ;15.499 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;21.340 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   192 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1454 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   250 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   409 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   937 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   660 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   649 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    63 ; 0.195 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    16 ; 0.166 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.139 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    30 ; 0.279 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.167 ; 0.200       
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):   832 ; 1.244 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   327 ; 0.320 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1276 ; 1.810 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   520 ; 3.013 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   451 ; 4.485 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4130  -4.0310  17.9680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1144 T22:   0.4711                                     
REMARK   3      T33:  -0.0416 T12:   0.0949                                     
REMARK   3      T13:  -0.0227 T23:  -0.0909                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8289 L22:   1.8661                                     
REMARK   3      L33:   3.4434 L12:  -3.0475                                     
REMARK   3      L13:  -1.9108 L23:  -0.7020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1775 S12:  -2.2159 S13:   0.4514                       
REMARK   3      S21:   0.3666 S22:   0.6046 S23:  -0.1247                       
REMARK   3      S31:  -0.4048 S32:  -0.1021 S33:  -0.4272                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A    95                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1900   8.6950   3.0140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1420 T22:  -0.1470                                     
REMARK   3      T33:   0.0023 T12:   0.0009                                     
REMARK   3      T13:  -0.0237 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8019 L22:   5.2158                                     
REMARK   3      L33:   7.4175 L12:   0.1178                                     
REMARK   3      L13:   2.9855 L23:   2.1627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1415 S12:   0.0340 S13:  -0.1205                       
REMARK   3      S21:  -0.0512 S22:   0.0399 S23:  -0.6263                       
REMARK   3      S31:  -0.2629 S32:   0.5229 S33:  -0.1814                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    96        A   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5270   2.2890   7.0410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1014 T22:  -0.1434                                     
REMARK   3      T33:  -0.0208 T12:   0.0250                                     
REMARK   3      T13:   0.0029 T23:   0.0858                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3081 L22:   2.3269                                     
REMARK   3      L33:   1.8259 L12:  -3.2728                                     
REMARK   3      L13:  -0.2863 L23:   0.9149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2787 S12:  -0.6455 S13:  -0.8690                       
REMARK   3      S21:   0.1819 S22:   0.2580 S23:   0.3541                       
REMARK   3      S31:   0.1946 S32:   0.1136 S33:   0.0206                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   875        B   894                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8740   3.7530  11.9340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0403 T22:  -0.0773                                     
REMARK   3      T33:  -0.0075 T12:   0.1197                                     
REMARK   3      T13:  -0.0322 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.4895 L22:   6.0209                                     
REMARK   3      L33:   4.0023 L12:  -0.7201                                     
REMARK   3      L13:  -2.9325 L23:   1.0760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1725 S12:  -0.7766 S13:   0.7098                       
REMARK   3      S21:   0.6035 S22:   0.3925 S23:  -0.6681                       
REMARK   3      S31:  -0.4301 S32:  -0.1298 S33:  -0.2200                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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                                                           
REMARK   4                                                                      
REMARK   4 3BYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046107.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14639                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1IWQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-19% PEG 3350, 0.120MM AMMONIUM        
REMARK 280  PHOSPHATE, 15% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K, PH 7                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       33.88400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.36850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       33.88400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.36850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE MONOMER CONTAINED IN THE      
REMARK 300 ASYMMETRIC UNIT                                                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3080 ANGSTROM**2                          
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 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      HOH A 153  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 223  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     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     MET A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     ARG B   895                                                      
REMARK 465     SER B   896                                                      
REMARK 465     SER B   897                                                      
REMARK 465     LYS B   898                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    45     O    HOH A   220              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  45   CD    GLU A  45   OE2     0.070                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A  36   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS B 876       23.25    -67.51                                   
REMARK 500    ARG B 893       35.70    -94.58                                   
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 152  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  87.6                                              
REMARK 620 3 ASP A  24   OD1  90.5  80.0                                        
REMARK 620 4 THR A  26   O    79.6 159.0  83.5                                  
REMARK 620 5 GLU A  31   OE1 106.2 128.0 146.9  72.1                            
REMARK 620 6 GLU A  31   OE2  95.1  78.4 157.4 119.1  51.1                      
REMARK 620 7 HOH A 176   O   164.9  77.9  82.9 112.9  86.3  86.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 151  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  83.0                                              
REMARK 620 3 ASN A  60   OD1  87.1  76.0                                        
REMARK 620 4 THR A  62   O    75.1 150.8  83.8                                  
REMARK 620 5 GLU A  67   OE1  71.6 118.6 151.4  72.6                            
REMARK 620 6 GLU A  67   OE2  85.3  76.5 152.2 119.8  47.2                      
REMARK 620 7 HOH A 226   O   167.5  85.2  86.0 114.3 118.2  96.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 150  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  85.6                                              
REMARK 620 3 ASN A  97   OD1  86.6  77.7                                        
REMARK 620 4 TYR A  99   O    85.9 154.2  77.5                                  
REMARK 620 5 GLU A 104   OE1 105.8 127.9 151.5  77.9                            
REMARK 620 6 GLU A 104   OE2 100.3  74.6 150.8 131.0  53.4                      
REMARK 620 7 HOH A 157   O   164.2  79.5  85.4 105.5  87.5  80.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 149  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  82.9                                              
REMARK 620 3 ASP A 133   OD1  96.9  79.4                                        
REMARK 620 4 GLN A 135   O    86.4 156.4  81.1                                  
REMARK 620 5 GLU A 140   OE1 107.2 124.4 147.3  78.9                            
REMARK 620 6 GLU A 140   OE2  82.8  77.7 156.9 121.8  51.1                      
REMARK 620 7 HOH A 156   O   166.1  83.6  77.5 105.0  83.1  97.3                
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 149                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HQW   RELATED DB: PDB                                   
REMARK 900 A STRUCTURE OF THE SAME COMPLEX IN A DIFFERENCE SPACE GROUP          
REMARK 900 RELATED ID: 1EXR   RELATED DB: PDB                                   
REMARK 900 A HIGH RESOLUTION STRUCTURE OF CALMODULIN                            
DBREF  3BYA A    1   148  UNP    P62158   CALM_HUMAN       2    149             
DBREF  3BYA B  875   898  UNP    Q05586   NMDZ1_HUMAN    875    898             
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   24  LYS LYS LYS ALA THR PHE ARG ALA ILE THR SER THR LEU          
SEQRES   2 B   24  ALA SER SER PHE LYS ARG ARG ARG SER SER LYS                  
HET     CA  A 149       1                                                       
HET     CA  A 150       1                                                       
HET     CA  A 151       1                                                       
HET     CA  A 152       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *79(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  GLU A   54  1                                  11    
HELIX    4   4 ASP A   64  MET A   72  1                                   9    
HELIX    5   5 SER A   81  ASP A   93  1                                  13    
HELIX    6   6 SER A  101  GLY A  113  1                                  13    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  THR A  146  1                                   9    
HELIX    9   9 LYS B  876  ARG B  893  1                                  18    
SHEET    1   A 2 TYR A  99  ILE A 100  0                                        
SHEET    2   A 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 152     1555   1555  2.07  
LINK         OD1 ASP A  22                CA    CA A 152     1555   1555  2.15  
LINK         OD1 ASP A  24                CA    CA A 152     1555   1555  2.44  
LINK         O   THR A  26                CA    CA A 152     1555   1555  2.17  
LINK         OE1 GLU A  31                CA    CA A 152     1555   1555  2.53  
LINK         OE2 GLU A  31                CA    CA A 152     1555   1555  2.51  
LINK         OD1 ASP A  56                CA    CA A 151     1555   1555  2.40  
LINK         OD1 ASP A  58                CA    CA A 151     1555   1555  2.34  
LINK         OD1 ASN A  60                CA    CA A 151     1555   1555  2.11  
LINK         O   THR A  62                CA    CA A 151     1555   1555  2.37  
LINK         OE1 GLU A  67                CA    CA A 151     1555   1555  2.84  
LINK         OE2 GLU A  67                CA    CA A 151     1555   1555  2.63  
LINK         OD1 ASP A  93                CA    CA A 150     1555   1555  2.30  
LINK         OD1 ASP A  95                CA    CA A 150     1555   1555  2.33  
LINK         OD1 ASN A  97                CA    CA A 150     1555   1555  2.40  
LINK         O   TYR A  99                CA    CA A 150     1555   1555  2.35  
LINK         OE1 GLU A 104                CA    CA A 150     1555   1555  2.43  
LINK         OE2 GLU A 104                CA    CA A 150     1555   1555  2.50  
LINK         OD1 ASP A 129                CA    CA A 149     1555   1555  2.31  
LINK         OD1 ASP A 131                CA    CA A 149     1555   1555  2.37  
LINK         OD1 ASP A 133                CA    CA A 149     1555   1555  2.34  
LINK         O   GLN A 135                CA    CA A 149     1555   1555  2.28  
LINK         OE1 GLU A 140                CA    CA A 149     1555   1555  2.46  
LINK         OE2 GLU A 140                CA    CA A 149     1555   1555  2.60  
LINK        CA    CA A 149                 O   HOH A 156     1555   1555  2.38  
LINK        CA    CA A 150                 O   HOH A 157     1555   1555  2.43  
LINK        CA    CA A 151                 O   HOH A 226     1555   1555  2.97  
LINK        CA    CA A 152                 O   HOH A 176     1555   1555  2.43  
SITE     1 AC1  5 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC1  5 GLU A 140                                                     
SITE     1 AC2  5 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC2  5 GLU A 104                                                     
SITE     1 AC3  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC3  5 GLU A  67                                                     
SITE     1 AC4  5 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC4  5 GLU A  31                                                     
CRYST1   67.768   42.737   62.012  90.00 106.92  90.00 C 1 2 1       4          
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      0.014756  0.000000  0.004489        0.00000                         
SCALE2      0.000000  0.023399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016855        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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