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Database: PDB
Entry: 5JQA
LinkDB: 5JQA
Original site: 5JQA 
HEADER    CALCIUM BINDING PROTEIN/PROTEIN BINDING 04-MAY-16   5JQA              
TITLE     CAM:RM20 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: MYOSIN LIGHT CHAIN KINASE, SMOOTH MUSCLE;                  
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 1691-1710;                                    
COMPND  10 SYNONYM: SMMLCK, KINASE-RELATED PROTEIN, KRP, TELOKIN;               
COMPND  11 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, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE   6 CAM3, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    CALMODULIN, CALCIUM SIGNAL TRANSDUCTION, PROTEIN KINASE, MYOSIN LIGHT 
KEYWDS   2 CHAIN KINASE, CALCIUM BINDING PROTEIN-PROTEIN BINDING COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.L.TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON                       
REVDAT   2   27-SEP-23 5JQA    1       REMARK                                   
REVDAT   1   11-OCT-17 5JQA    0                                                
JRNL        AUTH   V.L.TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON              
JRNL        TITL   CAM:RM20 COMPLEX                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12699                          
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 658                             
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 910                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.26000                                              
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.18000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.142         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.796         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1464 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1380 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1971 ; 1.357 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3195 ; 0.819 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   187 ; 3.161 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;27.065 ;25.432       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   293 ;10.642 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;15.705 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   209 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1725 ; 0.022 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   327 ; 0.018 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   725 ; 2.087 ; 1.866       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   723 ; 2.075 ; 1.857       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   919 ; 3.257 ; 2.758       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   920 ; 3.257 ; 2.763       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   739 ; 2.742 ; 2.256       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   740 ; 2.740 ; 2.259       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1053 ; 4.481 ; 3.232       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1972 ; 7.066 ;15.947       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1907 ; 7.004 ;15.478       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    77                          
REMARK   3    RESIDUE RANGE :   A   401        A   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9266   1.2518  -7.7556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0164 T22:   0.0519                                     
REMARK   3      T33:   0.0371 T12:   0.0255                                     
REMARK   3      T13:  -0.0042 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5434 L22:   0.4639                                     
REMARK   3      L33:   1.1206 L12:  -0.3393                                     
REMARK   3      L13:   0.7699 L23:  -0.4013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0695 S12:  -0.0729 S13:  -0.0108                       
REMARK   3      S21:   0.0507 S22:   0.0699 S23:   0.0122                       
REMARK   3      S31:  -0.0978 S32:  -0.0919 S33:  -0.0003                       
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 :   A    78        A   148                          
REMARK   3    RESIDUE RANGE :   A   403        A   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3731 -17.5265 -14.1849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0167 T22:   0.0459                                     
REMARK   3      T33:   0.0337 T12:  -0.0057                                     
REMARK   3      T13:  -0.0126 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9014 L22:   0.5276                                     
REMARK   3      L33:   0.1594 L12:   0.0534                                     
REMARK   3      L13:  -0.0700 L23:  -0.1296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0088 S12:  -0.0368 S13:   0.0725                       
REMARK   3      S21:  -0.0134 S22:  -0.0003 S23:  -0.0078                       
REMARK   3      S31:   0.0346 S32:  -0.0134 S33:   0.0091                       
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 :   B     1        B    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2795  -7.3740  -7.1853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0113 T22:   0.0573                                     
REMARK   3      T33:   0.0402 T12:  -0.0048                                     
REMARK   3      T13:  -0.0091 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8862 L22:   1.4657                                     
REMARK   3      L33:   1.4010 L12:  -1.8709                                     
REMARK   3      L13:  -1.6074 L23:   0.6855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0578 S12:  -0.0137 S13:   0.0596                       
REMARK   3      S21:  -0.0004 S22:   0.0540 S23:  -0.0699                       
REMARK   3      S31:   0.0872 S32:  -0.0658 S33:   0.0038                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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                                                           
REMARK   4                                                                      
REMARK   4 5JQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220969.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND(111)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15660                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 96.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 2O5G                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6, 25% W/V    
REMARK 280  PEG4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       28.52400            
REMARK 290   SMTRY3   2  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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     0                                                      
REMARK 465     ALA A     1                                                      
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   NH2  ARG A    37     O    HOH A   501              2.03            
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    MET A  76      -64.03   -122.32                                   
REMARK 500    LYS A  77       95.83     85.98                                   
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 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  83.2                                              
REMARK 620 3 ASP A  24   OD1  83.7  81.0                                        
REMARK 620 4 THR A  26   O    83.7 158.5  80.7                                  
REMARK 620 5 GLU A  31   OE1 110.6 126.5 149.2  74.3                            
REMARK 620 6 GLU A  31   OE2  99.0  74.1 154.4 124.9  53.1                      
REMARK 620 7 HOH A 565   O   161.3  79.5  86.7 110.5  85.5  83.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  79.2                                              
REMARK 620 3 ASN A  60   OD1  84.3  73.4                                        
REMARK 620 4 THR A  62   O    88.9 152.6  81.0                                  
REMARK 620 5 GLU A  67   OE1 104.9 125.0 160.3  81.8                            
REMARK 620 6 GLU A  67   OE2  91.1  75.5 148.9 129.8  49.9                      
REMARK 620 7 HOH A 575   O   161.5  82.3  90.8 108.0  85.4  83.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  81.2                                              
REMARK 620 3 ASN A  97   OD1  83.0  74.9                                        
REMARK 620 4 TYR A  99   O    90.4 153.9  79.6                                  
REMARK 620 5 GLU A 104   OE1 110.6 130.9 151.2  75.2                            
REMARK 620 6 GLU A 104   OE2  96.7  78.5 153.2 127.2  53.4                      
REMARK 620 7 HOH A 541   O   161.1  80.8  86.9 103.5  85.7  85.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 404  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  81.3                                              
REMARK 620 3 ASP A 133   OD1  81.4  81.5                                        
REMARK 620 4 GLN A 135   O    84.0 156.7  78.5                                  
REMARK 620 5 GLU A 140   OE1 116.5 121.5 151.4  81.4                            
REMARK 620 6 GLU A 140   OE2  86.3  75.9 155.6 121.1  52.6                      
REMARK 620 7 HOH A 521   O   156.2  83.5  78.4 103.9  87.0 107.6                
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404                  
DBREF  5JQA A    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  5JQA B    1    20  UNP    Q15746   MYLK_HUMAN    1691   1710             
SEQADV 5JQA NH2 B   21  UNP  Q15746              AMIDATION                      
SEQRES   1 A  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 B   21  ARG ARG LYS TRP GLN LYS THR GLY ASN ALA VAL ARG ALA          
SEQRES   2 B   21  ILE GLY ARG LEU SER SER MET NH2                              
HET    NH2  B  21       1                                                       
HET     CA  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     CA  A 403       1                                                       
HET     CA  A 404       1                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NH2    H2 N                                                         
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *155(H2 O)                                                    
HELIX    1 AA1 THR A    5  ASP A   20  1                                  16    
HELIX    2 AA2 THR A   28  LEU A   39  1                                  12    
HELIX    3 AA3 THR A   44  GLU A   54  1                                  11    
HELIX    4 AA4 PHE A   65  ARG A   74  1                                  10    
HELIX    5 AA5 ASP A   80  ASP A   93  1                                  14    
HELIX    6 AA6 SER A  101  LEU A  112  1                                  12    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 TYR A  138  THR A  146  1                                   9    
HELIX    9 AA9 ARG B    2  MET B   20  1                                  19    
SHEET    1 AA1 2 THR A  26  ILE A  27  0                                        
SHEET    2 AA1 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1 AA2 2 TYR A  99  ILE A 100  0                                        
SHEET    2 AA2 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         C   MET B  20                 N   NH2 B  21     1555   1555  1.34  
LINK         OD1 ASP A  20                CA    CA A 401     1555   1555  2.24  
LINK         OD1 ASP A  22                CA    CA A 401     1555   1555  2.42  
LINK         OD1 ASP A  24                CA    CA A 401     1555   1555  2.36  
LINK         O   THR A  26                CA    CA A 401     1555   1555  2.34  
LINK         OE1 GLU A  31                CA    CA A 401     1555   1555  2.42  
LINK         OE2 GLU A  31                CA    CA A 401     1555   1555  2.52  
LINK         OD1 ASP A  56                CA    CA A 402     1555   1555  2.24  
LINK         OD1 ASP A  58                CA    CA A 402     1555   1555  2.48  
LINK         OD1 ASN A  60                CA    CA A 402     1555   1555  2.33  
LINK         O   THR A  62                CA    CA A 402     1555   1555  2.33  
LINK         OE1 GLU A  67                CA    CA A 402     1555   1555  2.55  
LINK         OE2 GLU A  67                CA    CA A 402     1555   1555  2.69  
LINK         OD1 ASP A  93                CA    CA A 403     1555   1555  2.28  
LINK         OD1 ASP A  95                CA    CA A 403     1555   1555  2.40  
LINK         OD1 ASN A  97                CA    CA A 403     1555   1555  2.45  
LINK         O   TYR A  99                CA    CA A 403     1555   1555  2.26  
LINK         OE1 GLU A 104                CA    CA A 403     1555   1555  2.43  
LINK         OE2 GLU A 104                CA    CA A 403     1555   1555  2.53  
LINK         OD1 ASP A 129                CA    CA A 404     1555   1555  2.35  
LINK         OD1 ASP A 131                CA    CA A 404     1555   1555  2.28  
LINK         OD1 ASP A 133                CA    CA A 404     1555   1555  2.46  
LINK         O   GLN A 135                CA    CA A 404     1555   1555  2.29  
LINK         OE1 GLU A 140                CA    CA A 404     1555   1555  2.40  
LINK         OE2 GLU A 140                CA    CA A 404     1555   1555  2.59  
LINK        CA    CA A 401                 O   HOH A 565     1555   1555  2.30  
LINK        CA    CA A 402                 O   HOH A 575     1555   1555  2.12  
LINK        CA    CA A 403                 O   HOH A 541     1555   1555  2.52  
LINK        CA    CA A 404                 O   HOH A 521     1555   1555  2.35  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 565                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 575                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 541                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 521                                          
CRYST1   29.016   57.048   45.068  90.00  98.17  90.00 P 1 21 1      2          
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      0.034464  0.000000  0.004950        0.00000                         
SCALE2      0.000000  0.017529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022416        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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