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Database: PDB
Entry: 2WEL
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HEADER    TRANSFERASE                             31-MAR-09   2WEL              
TITLE     CRYSTAL STRUCTURE OF SU6656-BOUND CALCIUM/CALMODULIN-DEPENDENT PROTEIN
TITLE    2 KINASE II DELTA IN COMPLEX WITH CALMODULIN                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA  
COMPND   3 CHAIN;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: KINASE DOMAIN, RESIDUES 11-335;                            
COMPND   6 SYNONYM: CALCIUM CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA,  
COMPND   7 CAM-KINASE II DELTA CHAIN, CAM KINASE II SUBUNIT DELTA, CAMK-II      
COMPND   8 SUBUNIT DELTA;                                                       
COMPND   9 EC: 2.7.11.17;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: CALMODULIN;                                                
COMPND  13 CHAIN: D;                                                            
COMPND  14 SYNONYM: CAM;                                                        
COMPND  15 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_VARIANT: R3-PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;                              
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: R3-PRARE2;                                
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    CELLULAR DIFFERENTIATION, SERINE/THREONINE-PROTEIN KINASE,            
KEYWDS   2 PHOSPHOPROTEIN, CALMODULIN-BINDING, CALMODULIN BINDING, KINASE,      
KEYWDS   3 TRANSFERASE, ATP-BINDING, NUCLEOTIDE-BINDING, VASCULAR SMOOTH        
KEYWDS   4 MUSCLE, SERINE-THREONINE KINASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.W.PIKE,P.RELLOS,E.SALAH,N.BURGESS-BROWN,T.KEATES,J.MUNIZ,R.SETHI, 
AUTHOR   2 A.ROOS,P.FILIPPAKOPOULOS,F.VON DELFT,A.EDWARDS,J.WEIGELT,            
AUTHOR   3 C.H.ARROWSMITH,C.BOUNTRA,S.KNAPP                                     
REVDAT   4   24-JAN-18 2WEL    1       AUTHOR JRNL                              
REVDAT   3   10-AUG-11 2WEL    1       JRNL   REMARK HETSYN                     
REVDAT   2   13-JUL-11 2WEL    1       VERSN                                    
REVDAT   1   14-APR-09 2WEL    0                                                
JRNL        AUTH   P.RELLOS,A.C.W.PIKE,F.H.NIESEN,E.SALAH,W.H.LEE,F.VON DELFT,  
JRNL        AUTH 2 S.KNAPP                                                      
JRNL        TITL   STRUCTURE OF THE CAMKIIDELTA/CALMODULIN COMPLEX REVEALS THE  
JRNL        TITL 2 MOLECULAR MECHANISM OF CAMKII KINASE ACTIVATION.             
JRNL        REF    PLOS BIOL.                    V.   8   426 2010              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   20668654                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1000426                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 45074                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 827                             
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3286                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3544                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 405                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 20.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.92000                                             
REMARK   3    B22 (A**2) : 1.02000                                              
REMARK   3    B33 (A**2) : 0.90000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.114         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.064         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3702 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2529 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4991 ; 1.370 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6148 ; 0.911 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   446 ; 5.207 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;32.518 ;24.590       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   657 ;12.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;18.403 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   543 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4078 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   728 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   755 ; 0.216 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2422 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1791 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1772 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   330 ; 0.156 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.096 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    14 ; 0.163 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    16 ; 0.163 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    71 ; 0.170 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.230 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     1 ; 0.047 ; 0.200       
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):  2233 ; 3.306 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   909 ; 1.101 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3596 ; 4.709 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1469 ; 7.070 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1395 ; 9.372 ;11.000       
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  : 2                                          
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    -1        A   276                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2686 -14.5916 -13.2017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0060 T22:   0.0226                                     
REMARK   3      T33:   0.0759 T12:  -0.0012                                     
REMARK   3      T13:  -0.0061 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5099 L22:   0.4313                                     
REMARK   3      L33:   1.7413 L12:   0.0989                                     
REMARK   3      L13:  -0.2262 L23:  -0.1534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:   0.0163 S13:   0.0196                       
REMARK   3      S21:  -0.0411 S22:   0.0383 S23:   0.0360                       
REMARK   3      S31:  -0.0394 S32:  -0.1191 S33:  -0.0405                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D   147                          
REMARK   3    RESIDUE RANGE :   A   294        A   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.1056 -20.6549 -51.1215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1168 T22:   0.0936                                     
REMARK   3      T33:   0.0797 T12:   0.0058                                     
REMARK   3      T13:  -0.0190 T23:   0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2733 L22:   2.7636                                     
REMARK   3      L33:   1.2672 L12:  -0.5723                                     
REMARK   3      L13:   0.0713 L23:   0.5465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0305 S12:   0.2130 S13:   0.0167                       
REMARK   3      S21:  -0.3417 S22:   0.0074 S23:   0.1598                       
REMARK   3      S31:  -0.2259 S32:  -0.0702 S33:  -0.0379                       
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. U VALUES RESIDUAL ONLY.                                  
REMARK   4                                                                      
REMARK   4 2WEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290039286.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45901                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2VN9, 1MXE                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM POTASSIUM PHOSPHATE, 20%     
REMARK 280  PEG3350 10% ETHYLENE GLYCOL, PH 7.5                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.13000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.99000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.42500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.99000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.13000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.42500            
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 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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   277                                                      
REMARK 465     VAL A   278                                                      
REMARK 465     ALA A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     ALA A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     ASP A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     VAL A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     GLU A   329                                                      
REMARK 465     SER A   330                                                      
REMARK 465     THR A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D   148                                                      
REMARK 465     LYS D   149                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 276    OG                                                  
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     LYS A 293    CE   NZ                                             
REMARK 470     PHE A 314    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D   7    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  55    CD   OE1  OE2                                       
REMARK 470     ARG D  75    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  76    CG   CD   CE   NZ                                   
REMARK 470     LYS D  95    CD   CE   NZ                                        
REMARK 470     LYS D 116    CD   CE   NZ                                        
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   O    HOH D  2046     O    HOH D  2047              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2034     O    HOH A  2047     4545     2.06            
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    PHE A  17     -136.94   -121.60                                   
REMARK 500    GLU A 106      -56.46     74.94                                   
REMARK 500    ARG A 135       -3.91     70.57                                   
REMARK 500    ASP A 157       61.94     62.47                                   
REMARK 500    PHE A 233       78.33   -119.11                                   
REMARK 500    LEU A 253       48.22    -92.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2016        DISTANCE =  5.89 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 (2-OXO-3-(4,5,6,7-TETRAHYDRO-1 H-INDOL-2-YLMETHYLENE)-2,             
REMARK 600  3-DIHYDRO-1H-INDOLE-5-SULFONIC ACID DIMETHYLAMIDE) (K88):           
REMARK 600  SU6656                                                              
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 D 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  25   OD1                                                    
REMARK 620 2 ASP D  21   OD1  82.5                                              
REMARK 620 3 THR D  27   O    79.4  76.8                                        
REMARK 620 4 GLU D  32   OE1 150.2 109.7  77.3                                  
REMARK 620 5 ASP D  23   OD2  80.5  80.1 151.0 127.5                            
REMARK 620 6 GLU D  32   OE2 158.6  92.7 119.9  50.8  78.1                      
REMARK 620 7 HOH D2019   O    87.3 164.3 113.1  85.0  86.5  92.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  57   OD1                                                    
REMARK 620 2 ASP D  59   OD1  75.2                                              
REMARK 620 3 ASN D  61   OD1  91.3  80.7                                        
REMARK 620 4 THR D  63   O    86.8 153.6  80.6                                  
REMARK 620 5 GLU D  68   OE1  95.7 120.3 159.0  80.0                            
REMARK 620 6 GLU D  68   OE2  77.3  71.8 152.1 123.3  48.9                      
REMARK 620 7 HOH D2053   O   161.5  90.5  98.0 110.4  81.2  87.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN D  98   OD1                                                    
REMARK 620 2 TYR D 100   O    82.4                                              
REMARK 620 3 HOH D2104   O    81.0  81.7                                        
REMARK 620 4 ASP D  96   OD1  73.9 152.6 107.2                                  
REMARK 620 5 GLU D 105   OE2 149.1 128.2 105.7  75.3                            
REMARK 620 6 ASP D  94   OD1  83.6  83.2 159.7  80.8  94.3                      
REMARK 620 7 GLU D 105   OE1 159.3  78.1  89.3 126.8  51.4 100.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 132   OD1                                                    
REMARK 620 2 ASP D 134   OD1  82.2                                              
REMARK 620 3 GLN D 136   O   154.0  76.0                                        
REMARK 620 4 GLU D 141   OE2  75.7 157.9 125.3                                  
REMARK 620 5 GLU D 141   OE1 125.6 150.7  78.7  50.7                            
REMARK 620 6 HOH D2102   O    93.5  78.9  96.0 102.0  89.4                      
REMARK 620 7 ASP D 130   OD1  79.0  86.5  85.6  89.5 106.1 164.4                
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 K88 A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 603                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F3Z   RELATED DB: PDB                                   
REMARK 900 CALMODULIN/IQ-AA DOMAIN COMPLEX                                      
REMARK 900 RELATED ID: 1J7P   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF CALCIUM CALMODULIN C- TERMINAL DOMAIN          
REMARK 900 RELATED ID: 1NKF   RELATED DB: PDB                                   
REMARK 900 CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES                          
REMARK 900 RELATED ID: 2JL2   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX                   
REMARK 900 RELATED ID: 1K93   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EDEMA FACTOR COMPLEXED WITH CALMODULIN          
REMARK 900 RELATED ID: 1XFV   RELATED DB: PDB                                   
REMARK 900 FULL LENTH EF COMPLEXED CAM AND 3'-DEOXY- ATP                        
REMARK 900 RELATED ID: 1SK6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EF3/CALMODULIN COMPLEXED WITHCAMP/          
REMARK 900 PYROPHOSPHATE                                                        
REMARK 900 RELATED ID: 1Y6W   RELATED DB: PDB                                   
REMARK 900 TRAPPED INTERMEDIATE OF CALMODULIN                                   
REMARK 900 RELATED ID: 1IWQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MARCKS CALMODULIN BINDING DOMAINPEPTIDE         
REMARK 900 COMPLEXED WITH CA2+/CALMODULIN                                       
REMARK 900 RELATED ID: 1K90   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EDEMA FACTOR WITH CALMODULIN AND3'-DATP     
REMARK 900 RELATED ID: 1YRT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE ADENYLYL CYCLAESCATALYTIC DOMAIN   
REMARK 900 OF ADENYLYL CYCLASE TOXIN OF BORDETELLAPERTUSSIS IN PRESENCE OF C-   
REMARK 900 TERMINAL CALMODULIN                                                  
REMARK 900 RELATED ID: 1LVC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EF-CAM COMPLEXED WITH 3'-ANT-2'-DATP            
REMARK 900 RELATED ID: 2W73   RELATED DB: PDB                                   
REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE COMPLEX BETWEEN CALMODULIN AND A    
REMARK 900 PEPTIDE FROM CALCINEURIN A                                           
REMARK 900 RELATED ID: 1CLL   RELATED DB: PDB                                   
REMARK 900 CALMODULIN (VERTEBRATE)                                              
REMARK 900 RELATED ID: 1CDL   RELATED DB: PDB                                   
REMARK 900 CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTIDE FROM SMOOTH     
REMARK 900 MUSCLE MYOSIN LIGHT CHAIN KINASE                                     
REMARK 900 RELATED ID: 1XFY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FULLEF-CAM WITH 1 UM CALCIUM                    
REMARK 900 RELATED ID: 1XFU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-DELTA64 COMPLEX WITH CAM                
REMARK 900 RELATED ID: 2F3Y   RELATED DB: PDB                                   
REMARK 900 CALMODULIN/IQ DOMAIN COMPLEX                                         
REMARK 900 RELATED ID: 1XFX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-CAM COMPLEX AT 10 MM CALCIUM            
REMARK 900 RELATED ID: 1S26   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ANTHRAX EDEMA FACTOR-CALMODULIN- ALPHA,BETA-            
REMARK 900 METHYLENEADENOSINE 5'-TRIPHOSPHATE COMPLEX REVEALS ANALTERNATIVE     
REMARK 900 MODE OF ATP BINDING TO THE CATALYTIC SITE                            
REMARK 900 RELATED ID: 1J7O   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN N- TERMINAL DOMAIN          
REMARK 900 RELATED ID: 2W2C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM-   
REMARK 900 CALMODULIN DEPENDENT PROTEIN KINASE II DELTA                         
REMARK 900 RELATED ID: 2VN9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CALCIUM CALMODULIN DEPENDENT PROTEIN      
REMARK 900 KINASE II DELTA ISOFORM 1, CAMKD                                     
REMARK 900 RELATED ID: 1YRU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE ADENYLYL CYCLAESCATALYTIC DOMAIN   
REMARK 900 OF ADENYLYL CYCLASE TOXIN OF BORDETELLAPERTUSSIS IN PRESENCE OF C-   
REMARK 900 TERMINAL CALMODULIN AND 1MMCALCIUM CHLORIDE                          
REMARK 900 RELATED ID: 1WRZ   RELATED DB: PDB                                   
REMARK 900 CALMODULIN COMPLEXED WITH A PEPTIDE FROM A HUMAN DEATH-ASSOCIATED    
REMARK 900 PROTEIN KINASE                                                       
REMARK 900 RELATED ID: 2V02   RELATED DB: PDB                                   
REMARK 900 RECOMBINANT VERTEBRATE CALMODULIN COMPLEXED WITH BA                  
REMARK 900 RELATED ID: 1XFZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FULLEF-CAM WITH 1 MM CALCIUM                    
REMARK 900 RELATED ID: 1XFW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-CAM COMPLEXED WITH CAMP                 
REMARK 900 RELATED ID: 2V01   RELATED DB: PDB                                   
REMARK 900 RECOMBINANT VERTEBRATE CALMODULIN COMPLEXED WITH PB                  
REMARK 900 RELATED ID: 1PK0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EF3-CAM COMPLEXED WITH PMEAPP               
REMARK 900 RELATED ID: 2BE6   RELATED DB: PDB                                   
REMARK 900 2.0 A CRYSTAL STRUCTURE OF THE CAV1.2 IQ DOMAIN-CA/CAMCOMPLEX        
REMARK 900 RELATED ID: 1ZOT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE CYAA/C- CAM WITH PMEAPP            
REMARK 900 RELATED ID: 2VAY   RELATED DB: PDB                                   
REMARK 900 CALMODULIN COMPLEXED WITH CAV1.1 IQ PEPTIDE                          
REMARK 900 RELATED ID: 1SW8   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN N60DCALMODULIN  
REMARK 900 REFINED WITH PARAMAGNETISM BASED STRATEGY                            
REMARK 900 RELATED ID: 1AJI   RELATED DB: PDB                                   
REMARK 900 APO-CALMODULIN IN COMPLEX WITH BRUSH BORDER MYOSIN I IQ MOTIF,       
REMARK 900 THEORETICAL MODEL                                                    
DBREF  2WEL A   -1     0  PDB    2WEL     2WEL            -1      0             
DBREF  2WEL A   11   335  UNP    Q13557   KCC2D_HUMAN     11    335             
DBREF  2WEL D   -1    -1  PDB    2WEL     2WEL            -1     -1             
DBREF  2WEL D    1   149  UNP    P62158   CALM_HUMAN       1    149             
SEQRES   1 A  327  SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY          
SEQRES   2 A  327  LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE          
SEQRES   3 A  327  PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR          
SEQRES   4 A  327  LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG          
SEQRES   5 A  327  GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE          
SEQRES   6 A  327  VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS          
SEQRES   7 A  327  TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE          
SEQRES   8 A  327  GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP          
SEQRES   9 A  327  ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN          
SEQRES  10 A  327  HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  11 A  327  PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA          
SEQRES  12 A  327  ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL          
SEQRES  13 A  327  GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR          
SEQRES  14 A  327  PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO          
SEQRES  15 A  327  TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE          
SEQRES  16 A  327  LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP          
SEQRES  17 A  327  GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY          
SEQRES  18 A  327  ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR          
SEQRES  19 A  327  PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE          
SEQRES  20 A  327  ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS          
SEQRES  21 A  327  HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET          
SEQRES  22 A  327  MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE          
SEQRES  23 A  327  ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR          
SEQRES  24 A  327  MET LEU ALA THR ARG ASN PHE SER ALA ALA LYS SER LEU          
SEQRES  25 A  327  LEU LYS LYS PRO ASP GLY VAL LYS GLU SER THR GLU SER          
SEQRES  26 A  327  SER ASN                                                      
SEQRES   1 D  150  SER MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU          
SEQRES   2 D  150  PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP          
SEQRES   3 D  150  GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG          
SEQRES   4 D  150  SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP          
SEQRES   5 D  150  MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE          
SEQRES   6 D  150  ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET          
SEQRES   7 D  150  LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE          
SEQRES   8 D  150  ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA          
SEQRES   9 D  150  ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS          
SEQRES  10 D  150  LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA          
SEQRES  11 D  150  ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE          
SEQRES  12 D  150  VAL GLN MET MET THR ALA LYS                                  
HET    K88  A 600      26                                                       
HET    EDO  A 700       4                                                       
HET    EDO  A 701       4                                                       
HET    EDO  A 702       4                                                       
HET    EDO  A 703       4                                                       
HET    EDO  A 704       4                                                       
HET    EDO  A 705       4                                                       
HET    PO4  A 706       5                                                       
HET    PO4  A 707       5                                                       
HET     CA  D 600       1                                                       
HET     CA  D 601       1                                                       
HET     CA  D 602       1                                                       
HET     CA  D 603       1                                                       
HETNAM     K88 (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-          
HETNAM   2 K88  2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  K88    C19 H21 N3 O3 S                                              
FORMUL   4  EDO    6(C2 H6 O2)                                                  
FORMUL  10  PO4    2(O4 P 3-)                                                   
FORMUL  12   CA    4(CA 2+)                                                     
FORMUL  16  HOH   *405(H2 O)                                                    
HELIX    1   1 SER A   -1  GLU A   13  1                                   5    
HELIX    2   2 LYS A   48  LEU A   50  5                                   3    
HELIX    3   3 SER A   51  LEU A   68  1                                  18    
HELIX    4   4 GLU A   97  GLU A  106  1                                  10    
HELIX    5   5 SER A  109  ASN A  130  1                                  22    
HELIX    6   6 LYS A  138  GLU A  140  5                                   3    
HELIX    7   7 ASP A  157  ALA A  161  5                                   5    
HELIX    8   8 THR A  177  LEU A  181  5                                   5    
HELIX    9   9 SER A  182  ARG A  187  1                                   6    
HELIX   10  10 LYS A  193  GLY A  210  1                                  18    
HELIX   11  11 ASP A  218  GLY A  229  1                                  12    
HELIX   12  12 THR A  242  LEU A  253  1                                  12    
HELIX   13  13 THR A  262  LEU A  267  1                                   6    
HELIX   14  14 HIS A  269  GLN A  274  1                                   6    
HELIX   15  15 ASN A  295  ALA A  316  1                                  22    
HELIX   16  16 THR D    6  ASP D   21  1                                  16    
HELIX   17  17 THR D   29  LEU D   40  1                                  12    
HELIX   18  18 THR D   45  ASP D   57  1                                  13    
HELIX   19  19 ASP D   65  ALA D   74  1                                  10    
HELIX   20  20 LYS D   78  ASP D   94  1                                  17    
HELIX   21  21 SER D  102  LEU D  113  1                                  12    
HELIX   22  22 THR D  118  ASP D  130  1                                  13    
HELIX   23  23 TYR D  139  MET D  146  1                                   8    
SHEET    1  AA 5 TYR A  14  GLY A  23  0                                        
SHEET    2  AA 5 SER A  26  LYS A  33 -1  O  SER A  26   N  GLY A  23           
SHEET    3  AA 5 GLU A  39  ASN A  46 -1  O  TYR A  40   N  CYS A  31           
SHEET    4  AA 5 PHE A  85  PHE A  90 -1  O  HIS A  86   N  ILE A  45           
SHEET    5  AA 5 LEU A  76  GLU A  82 -1  N  HIS A  77   O  VAL A  89           
SHEET    1  AB 2 ILE A 132  VAL A 133  0                                        
SHEET    2  AB 2 ILE A 162  GLU A 163 -1  O  ILE A 162   N  VAL A 133           
SHEET    1  AC 2 LEU A 142  LEU A 144  0                                        
SHEET    2  AC 2 VAL A 153  LEU A 155 -1  O  LYS A 154   N  LEU A 143           
SHEET    1  DA 2 TYR D 100  ILE D 101  0                                        
SHEET    2  DA 2 VAL D 137  ASN D 138 -1  O  VAL D 137   N  ILE D 101           
LINK        CA    CA D 600                 OD1 ASP D  25     1555   1555  2.49  
LINK        CA    CA D 600                 OD1 ASP D  21     1555   1555  2.18  
LINK        CA    CA D 600                 O   THR D  27     1555   1555  2.35  
LINK        CA    CA D 600                 OE1 GLU D  32     1555   1555  2.60  
LINK        CA    CA D 600                 OD2 ASP D  23     1555   1555  2.31  
LINK        CA    CA D 600                 OE2 GLU D  32     1555   1555  2.61  
LINK        CA    CA D 600                 O   HOH D2019     1555   1555  2.37  
LINK        CA    CA D 601                 OD1 ASP D  57     1555   1555  2.15  
LINK        CA    CA D 601                 OD1 ASP D  59     1555   1555  2.51  
LINK        CA    CA D 601                 OD1 ASN D  61     1555   1555  2.36  
LINK        CA    CA D 601                 O   THR D  63     1555   1555  2.45  
LINK        CA    CA D 601                 OE1 GLU D  68     1555   1555  2.47  
LINK        CA    CA D 601                 OE2 GLU D  68     1555   1555  2.75  
LINK        CA    CA D 601                 O   HOH D2053     1555   1555  2.05  
LINK        CA    CA D 602                 OD1 ASN D  98     1555   1555  2.44  
LINK        CA    CA D 602                 O   TYR D 100     1555   1555  2.25  
LINK        CA    CA D 602                 O   HOH D2104     1555   1555  2.51  
LINK        CA    CA D 602                 OD1 ASP D  96     1555   1555  2.36  
LINK        CA    CA D 602                 OE2 GLU D 105     1555   1555  2.47  
LINK        CA    CA D 602                 OD1 ASP D  94     1555   1555  2.28  
LINK        CA    CA D 602                 OE1 GLU D 105     1555   1555  2.48  
LINK        CA    CA D 603                 OD1 ASP D 132     1555   1555  2.40  
LINK        CA    CA D 603                 OD1 ASP D 134     1555   1555  2.44  
LINK        CA    CA D 603                 O   GLN D 136     1555   1555  2.37  
LINK        CA    CA D 603                 OE2 GLU D 141     1555   1555  2.44  
LINK        CA    CA D 603                 OE1 GLU D 141     1555   1555  2.54  
LINK        CA    CA D 603                 O   HOH D2102     1555   1555  2.40  
LINK        CA    CA D 603                 OD1 ASP D 130     1555   1555  2.25  
CISPEP   1 SER A  235    PRO A  236          0        -1.22                     
SITE     1 AC1 11 LEU A  20  VAL A  28  ALA A  41  LYS A  43                    
SITE     2 AC1 11 PHE A  90  ASP A  91  LEU A  92  VAL A  93                    
SITE     3 AC1 11 ASP A 157  EDO A 700  EDO A 701                               
SITE     1 AC2  3 K88 A 600  HOH A2289  HOH A2290                               
SITE     1 AC3  7 GLU A  61  VAL A  74  PHE A  90  ALA A 156                    
SITE     2 AC3  7 ASP A 157  PHE A 158  K88 A 600                               
SITE     1 AC4  5 GLU A 140  TYR A 180  HIS A 283  GLN A 285                    
SITE     2 AC4  5 HOH A2292                                                     
SITE     1 AC5  4 HIS A  55  SER A  81  LYS A 147  PO4 A 706                    
SITE     1 AC6  7 TYR A  14  LYS A  33  HIS A  77  PO4 A 707                    
SITE     2 AC6  7 HOH A2089  HOH A2293  HOH D2092                               
SITE     1 AC7  5 TYR A 205  PRO A 213  TYR A 231  ASP A 232                    
SITE     2 AC7  5 HOH A2294                                                     
SITE     1 AC8 10 THR A  47  HIS A  55  SER A  81  GLU A  82                    
SITE     2 AC8 10 PHE A  85  HIS A  86  SER A 148  LYS A 149                    
SITE     3 AC8 10 EDO A 703  HOH A2295                                          
SITE     1 AC9  6 LYS A  69  ARG A  75  HIS A  77  EDO A 704                    
SITE     2 AC9  6 HOH A2089  HOH A2297                                          
SITE     1 BC1  6 ASP D  21  ASP D  23  ASP D  25  THR D  27                    
SITE     2 BC1  6 GLU D  32  HOH D2019                                          
SITE     1 BC2  6 ASP D  57  ASP D  59  ASN D  61  THR D  63                    
SITE     2 BC2  6 GLU D  68  HOH D2053                                          
SITE     1 BC3  6 ASP D  94  ASP D  96  ASN D  98  TYR D 100                    
SITE     2 BC3  6 GLU D 105  HOH D2104                                          
SITE     1 BC4  6 ASP D 130  ASP D 132  ASP D 134  GLN D 136                    
SITE     2 BC4  6 GLU D 141  HOH D2102                                          
CRYST1   68.260   68.850  121.980  90.00  90.00  90.00 P 21 21 21    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      0.014650  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014524  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008198        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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