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Database: PDB
Entry: 2LV6
LinkDB: 2LV6
Original site: 2LV6 
HEADER    METAL BINDING PROTEIN/TRANSFERASE       29-JUN-12   2LV6              
TITLE     THE COMPLEX BETWEEN CA-CALMODULIN AND SKELETAL MUSCLE MYOSIN LIGHT    
TITLE    2 CHAIN KINASE FROM COMBINATION OF NMR AND AQUEOUS AND CONTRAST-MATCHED
TITLE    3 SAXS DATA                                                            
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 2, SKELETAL/CARDIAC MUSCLE;      
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: CALMODULIN-BINDING RESIDUES 566-591;                       
COMPND  10 SYNONYM: MLCK2;                                                      
COMPND  11 EC: 2.7.11.18;                                                       
COMPND  12 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: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VARIANT: CODON-PLUS (DE3) RIPL;                    
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET21A;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    PB-SUBSTITUTED, PROTEIN COMPLEX, METAL BINDING PROTEIN-TRANSFERASE    
KEYWDS   2 COMPLEX                                                              
EXPDTA    SOLUTION SCATTERING; SOLUTION NMR                                     
AUTHOR    A.V.GRISHAEV,N.J.ANTHIS,G.M.CLORE                                     
REVDAT   2   27-MAR-13 2LV6    1       REMARK                                   
REVDAT   1   20-FEB-13 2LV6    0                                                
JRNL        AUTH   A.GRISHAEV,N.J.ANTHIS,G.M.CLORE                              
JRNL        TITL   CONTRAST-MATCHED SMALL-ANGLE X-RAY SCATTERING FROM A         
JRNL        TITL 2 HEAVY-ATOM-LABELED PROTEIN IN STRUCTURE DETERMINATION:       
JRNL        TITL 3 APPLICATION TO A LEAD-SUBSTITUTED CALMODULIN-PEPTIDE         
JRNL        TITL 4 COMPLEX.                                                     
JRNL        REF    J.AM.CHEM.SOC.                V. 134 14686 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   22908850                                                     
JRNL        DOI    10.1021/JA306359Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0, CUSTOM                                      
REMARK   3   AUTHORS     : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ (CNS)   
REMARK   3                 , GRISHAEV (CUSTOM)                                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RELATIVE POSITIONS OF THE N- AND C-       
REMARK   3  TERMINAL DOMAINS OF CALMODULIN, RIGIDLY HELD AT THOSE OF THE 1MXE   
REMARK   3  STRUCTURE, CHAIN A, WERE OPTIMIZED VIA A ROTATIONAL/TRANSLATIONAL   
REMARK   3  GRID SEARCH WITH STEPS OF 2DEG AND 1A, RESPECTIVELY WITH THE BEST   
REMARK   3  MODEL FITTED AGAINST RDC AND SCATTERING INTENSITY DATA.             
REMARK   3  COORDINATES OF THE CALMODULIN LINKER RESIDUES (76-81) AND THE       
REMARK   3  INTERFACIAL SIDE CHAINS WERE REGULARIZED VIA A MOLECULAR            
REMARK   3  DYNAMICS/SIMULATED ANNEALING PROTOCOL WITH THE BACKBONE ATOMS AND   
REMARK   3  THE REMAINING SIDE CHAINS HELD FIXED AT THE GEOMETRY RESULTING      
REMARK   3  FROM THE RIGID-BODY GRID SEARCH OF THE PREVIOUS STEP.               
REMARK   4                                                                      
REMARK   4 2LV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB102873.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 300; 300                           
REMARK 210  PH                             : 6.5; 6.5                           
REMARK 210  IONIC STRENGTH                 : 0.1; 0.15                          
REMARK 210  PRESSURE                       : AMBIENT; AMBIENT                   
REMARK 210  SAMPLE CONTENTS                : 0.3 MM [U-13C; U-15N; U-2H]        
REMARK 210                                   CALMODULIN, 0.3 MM SSMLCK, 95%     
REMARK 210                                   H2O/5% D2O; 0.06-0.25 MM [U-13C;   
REMARK 210                                   U-15N; U-2H] CALMODULIN, 0.06-     
REMARK 210                                   0.25 MM SSMLCK, 65% W/V SUCROSE/   
REMARK 210                                   H2O                                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC                     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE, SPARKY, CUSTOM            
REMARK 210   METHOD USED                   : RIGID-BODY OPTIMIZATION,           
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 1                                  
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 265                                                                      
REMARK 265 EXPERIMENTAL DETAILS                                                 
REMARK 265                                                                      
REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING                       
REMARK 265  DATA ACQUISITION                                                    
REMARK 265   RADIATION/NEUTRON SOURCE                 : ADVANCED PHOTON SOURCE  
REMARK 265   SYNCHROTRON (Y/N)                        : Y                       
REMARK 265   BEAMLINE TYPE                            : 12-IDB                  
REMARK 265   BEAMLINE INSTRUMENT                      : NULL                    
REMARK 265   DETECTOR TYPE                            : PILATUS 2M              
REMARK 265   DETECTOR MANUFACTURER DETAILS            : DECTRIS                 
REMARK 265   TEMPERATURE (KELVIN)                     : 298                     
REMARK 265   PH                                       : 6.5                     
REMARK 265   NUMBER OF TIME FRAMES USED               : 20                      
REMARK 265   PROTEIN CONCENTRATION RANGE (MG/ML)      : 1.2-5.0                 
REMARK 265   SAMPLE BUFFER                            : 25MM HEPES, 150 MM      
REMARK 265                                              KCL, 3 MM CACL2, 1 MM   
REMARK 265                                              TCEP, H2O               
REMARK 265   DATA REDUCTION SOFTWARE                  : MARDETECTOR, IGOR       
REMARK 265   GUINIER MEAN RADIUS OF GYRATION (NM)     : 1.78                    
REMARK 265   SIGMA MEAN RADIUS OF GYRATION            : 0.04                    
REMARK 265   R(XS-1) MEAN CROSS SECTIONAL RADII (NM)  : NULL                    
REMARK 265   R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL                    
REMARK 265   R(XS-2) MEAN CROSS SECTIONAL RADII (NM)  : NULL                    
REMARK 265   R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL                    
REMARK 265   P(R) PROTEIN LENGTH (NM)                 : 6.0                     
REMARK 265                                                                      
REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING                       
REMARK 265  DATA ACQUISITION                                                    
REMARK 265   RADIATION/NEUTRON SOURCE                 : ADVANCED PHOTON SOURCE  
REMARK 265   SYNCHROTRON (Y/N)                        : Y                       
REMARK 265   BEAMLINE TYPE                            : 12-IDC                  
REMARK 265   BEAMLINE INSTRUMENT                      : NULL                    
REMARK 265   DETECTOR TYPE                            : GOLD CCD                
REMARK 265   DETECTOR MANUFACTURER DETAILS            : NULL                    
REMARK 265   TEMPERATURE (KELVIN)                     : 298                     
REMARK 265   PH                                       : 6.5                     
REMARK 265   NUMBER OF TIME FRAMES USED               : 20                      
REMARK 265   PROTEIN CONCENTRATION RANGE (MG/ML)      : 5.0 - 9.5               
REMARK 265   SAMPLE BUFFER                            : 25MM HEPES, 150 MM      
REMARK 265                                              KCL, 1 MM TCEP, 3       
REMARK 265                                              MICROMOL PBCL2, 65%     
REMARK 265                                              SUCROSE, H2O            
REMARK 265   DATA REDUCTION SOFTWARE                  : MARDETECTOR, IGOR       
REMARK 265   GUINIER MEAN RADIUS OF GYRATION (NM)     : 1.8                     
REMARK 265   SIGMA MEAN RADIUS OF GYRATION            : 0.2                     
REMARK 265   R(XS-1) MEAN CROSS SECTIONAL RADII (NM)  : NULL                    
REMARK 265   R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL                    
REMARK 265   R(XS-2) MEAN CROSS SECTIONAL RADII (NM)  : NULL                    
REMARK 265   R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL                    
REMARK 265   P(R) PROTEIN LENGTH (NM)                 : NULL                    
REMARK 265                                                                      
REMARK 265 DATA ANALYSIS AND MODEL FITTING:                                     
REMARK 265  METHOD USED TO DETERMINE THE STRUCTURE: NULL                        
REMARK 265  SOFTWARE USED    : PRIMUS, GNOM                                     
REMARK 265  SOFTWARE AUTHORS : NULL                                             
REMARK 265  STARTING MODEL   : NULL                                             
REMARK 265                                                                      
REMARK 265 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 265 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 265 CONFORMERS, SELECTION CRITERIA  : BEST-FITTING CONFORMER BASED ON    
REMARK 265  THE FIT OF AQUEOUS SAXS DATA FOR CA-CAM/MLCK, CONTRAST-MATCHED      
REMARK 265  (65% SUCROSE) SAXS DATA FOR PB-CAM/MLCK, AND BACKBONE 1H-15N        
REMARK 265  RESIDUAL DIPOLAR COUPLINGS FOR CAM IN THE CA-CAM/MLCK COMPLEX       
REMARK 265                                                                      
REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 265                                                                      
REMARK 265  OTHER DETAILS: 4000000000000 STARTING RELATIVE POSITIONS OF THE N   
REMARK 265  -TERM (1-75) AND C-TERM (82-148) DOMAINS OF CAM WERE BUILT USING    
REMARK 265  COORDINATES IN THE PDB DEPOSITION 1MXE:A. TAIL RESIDUES 1-4 AND     
REMARK 265  144-148 WERE BEST-FITTED TO 1MXE USING MODELS 1J7O AND 1J7P.        
REMARK 265  THESE 4*1011 MODELS SAMPLE IN AN EXHAUSTIVE FASHION ALL POSSIBLE    
REMARK 265  RELATIVE DOMAIN POSITIONS WHICH DIFFER BY NO MORE THAN 1A IN        
REMARK 265  TERMS OF C-TERM DOMAIN PLACEMENT WHEN N-TERM DOMAIN IS FIXED.       
REMARK 265  ROTATIONAL AND TRANSLATIONAL GRIDS OF 2DEG AND 1A WERE USED. THE    
REMARK 265  MODELS WERE THEN FILTERED TO EXHIBIT FIT TO THE RDC DATA NO WORSE   
REMARK 265  THAN 10% HIGHER THAN GLOBAL MINIMUM FOUND BY NLS OPTIMIZATION OF    
REMARK 265  ORIENTATION OF THE C-TERM RELATIVE TO THE N-TERM DOMAIN.            
REMARK 265  ADDITIONAL FILTERS WERE THEN APPLIED INCLUDING ABSENCE OF CLASHES   
REMARK 265  <2.5 A BETWEEN HEAVY BACKBONE AND CB ATOMS, AND RGYR OF 13-19A.     
REMARK 265  FOR THE GEOMETRIES THAT PASSED ABOVE REQUIREMENTS, POSITION OF      
REMARK 265  MLCK FROM 2BBM DEPOSITION WAS BEST-FITTED IN A RIGID-BODY MANNER    
REMARK 265  AGAINST NOE DISTANCE RESTRAINTS FROM 2BBM DEPOSITION AND CLASH      
REMARK 265  AVOIDANCE FUNCTION INCLUDING HEAVY BACKBONE AND CB ATOMS. CAM       
REMARK 265  CONFORMATIONS WHICH EXHIBITED AT LEAST 1 NOE VIOLATION EXCEEDING    
REMARK 265  3A FOR THE BEST-FITTED MLCK WERE REJECTED. LINKER COORDINATES       
REMARK 265  WERE THEN BUILT FOR RESIDUES 76-81 USING 8-RESIDUE BACKBONE AND     
REMARK 265  CB-CONTAINING SEGMENTS FROM A PDB-BASED DATABASE INCLUDING 2.2      
REMARK 265  MILLION RESIDUES IN TOTAL. LINKERS WHICH CLASHED WITH CAM DOMAINS   
REMARK 265  OR MLCK OR EXHIBITED RMSD ABOVE 1.2 A FOR RESIDUES 1 AND 8 VS       
REMARK 265  RESIDUES 75 AND 82 OF CAM WERE REJECTED. CAM CONFORMATION FOR       
REMARK 265  WHICH SUCH LINKERS COULD NOT BE BUILT WERE REJECTED LEADING TO A    
REMARK 265  TOTAL OF APPROXIMATELY 75000 STRUCTURES. THESE STRUCTURES WERE      
REMARK 265  FITTED TO THE SAXS AND RDC DATA WITH THE OVERALL BEST-FITTING       
REMARK 265  MODEL RETAINED FOR DEPOSITION. THE COORDINATES OF THE LINKER        
REMARK 265  RESIDUES 76-81 AND SIDECHAINS WERE REGULARIZED BY ENERGY            
REMARK 265  MINIMIZATION VIA XPLOR-NIH PRIOR TO THE DEPOSITION WITH THE         
REMARK 265  ACTIVE ENERGY TERMS INCLUDING BONDS, ANGLES, IMPROPERS, NON-        
REMARK 265  BONDED, AND CONFORMATIONAL DATABASE POTENTIALS OF MEAN FORCE.       
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: 1442 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 2977 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.7 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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    VAL A   142     H    THR A   146              1.51            
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    THR A  79      -89.12     59.96                                   
REMARK 500    ASP A  80       37.00    170.10                                   
REMARK 500    SER A  81     -145.66     51.74                                   
REMARK 500    GLU A  82      -46.25    112.85                                   
REMARK 500    ALA A 147      169.99     59.61                                   
REMARK 500    SER B 221       91.37    -54.72                                   
REMARK 500    SER B 222       88.60    -55.37                                   
REMARK 500    SER B 223      102.93     25.31                                   
REMARK 500    ALA B 225      -38.60    -35.63                                   
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 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 GLN A 135   O    84.8                                              
REMARK 620 3 ASP A 133   OD1  86.8  78.8                                        
REMARK 620 4 GLU A 140   OE1 108.7  78.7 151.2                                  
REMARK 620 5 ASP A 131   OD1  89.4 154.0  75.7 126.9                            
REMARK 620 6 GLU A 140   OE2  91.4 125.5 155.5  51.3  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 PHE A  99   O    84.2                                              
REMARK 620 3 ASP A  95   OD1  82.8 153.5                                        
REMARK 620 4 GLU A 104   OE1 103.4  77.3 128.2                                  
REMARK 620 5 ASN A  97   OD1  87.0  77.7  78.7 151.7                            
REMARK 620 6 GLU A 104   OE2  99.4 128.4  76.5  51.6 153.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  81.3                                              
REMARK 620 3 ASN A  60   OD1  84.8  77.8                                        
REMARK 620 4 THR A  62   O    87.2 155.3  79.5                                  
REMARK 620 5 GLU A  67   OE1 106.0 124.2 156.2  79.9                            
REMARK 620 6 GLU A  67   OE2  89.2  74.8 152.6 127.0  50.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  26   O                                                      
REMARK 620 2 ASP A  24   OD1  85.7                                              
REMARK 620 3 ASP A  22   OD1 157.4  82.6                                        
REMARK 620 4 ASP A  20   OD1  82.3  90.2  78.5                                  
REMARK 620 5 GLU A  31   OE2 116.6 157.7  76.5  93.1                            
REMARK 620 6 GLU A  31   OE1  72.4 145.4 126.2 112.4  51.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MXE   RELATED DB: PDB                                   
REMARK 900 BACKBONE COORDINATES OF THE N- AND C-TERMINAL DOMAINS FROM           
REMARK 900 THIS ENTRY (RESIDUES 5-75 AND 82-146, RESPECTIVELY) WERE             
REMARK 900 USED DURING RIGID-BODY OPTIMIZATION OF THE GEOMETRY OF THE           
REMARK 900 CAM/MLCK COMPLEX.                                                    
REMARK 900 RELATED ID: 2BBM   RELATED DB: PDB                                   
REMARK 900 SKMLCK PEPTIDE COORDINATES AND DISTANCE RESTRAINTS FROM              
REMARK 900 THIS ENTRY WERE USED DURING RIGID-BODY OPTIMIZATION OF THE           
REMARK 900 GEOMETRY OF THE CAM/MLCK COMPLEX.                                    
REMARK 900 RELATED ID: 18556   RELATED DB: BMRB                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS DEPOSITED STRUCTURE OF HUMAN CALMODULIN WAS REFINED USING       
REMARK 999 INDIVIDUAL DOMAIN COORDINATES OF DEPOSITION 1MXE, WHICH CORRESPONDS  
REMARK 999 TO THE CHICKEN CALMODULIN. THE SEQUENCES OF HUMAN AND CHICKEN        
REMARK 999 CALMODULIN DIFFER IN TWO POSITIONS, 99 (TYR FOR HUMAN AND PHE FOR    
REMARK 999 CHICKEN) AND 143 (GLN FOR HUMAN AND THR FOR CHICKEN). THEREFORE,     
REMARK 999 THE SIDECHAIN COORDINATES OF RESIDUES 99 AND 143 IN THIS DEPOSITION  
REMARK 999 DO NOT REPRESENT COMPOSITION OF THE SAMPLES USED FOR EXPERIMENTAL    
REMARK 999 DATA COLLECTION. THIS DISCREPANCIES DO NOT PRODUCE ANY DIFFERENCES   
REMARK 999 WHEN EXPERIMENTAL DATA ARE FITTED SINCE BACKBONE N-HN RDC AND        
REMARK 999 CONTRAST-MATCHED SAXS DATA DO NOT INVOLVE THE SIDECHAIN COORDINATES  
REMARK 999 AND THEIR IMPACT ON THE AQUEOUS SAXS DATA IS NEGLIGIBLE.             
DBREF  2LV6 A    1   148  UNP    P62158   CALM_HUMAN       2    149             
DBREF  2LV6 B  201   226  UNP    Q9H1R3   MYLK2_HUMAN    566    591             
SEQADV 2LV6 PHE A   99  UNP  P62158    TYR   100 SEE REMARK 999                 
SEQADV 2LV6 THR A  143  UNP  P62158    GLN   144 SEE REMARK 999                 
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL THR          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   26  LYS ARG ARG TRP LYS LYS ASN PHE ILE ALA VAL SER ALA          
SEQRES   2 B   26  ALA ASN ARG PHE LYS LYS ILE SER SER SER GLY ALA LEU          
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 PHE A   65  ASP A   78  1                                  14    
HELIX    5   5 GLU A   82  ASP A   93  1                                  12    
HELIX    6   6 SER A  101  LEU A  112  1                                  12    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  ALA A  147  1                                  10    
HELIX    9   9 ARG B  203  ILE B  220  1                                  18    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 PHE A  99  ILE A 100  0                                        
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A 129                CA    CA A 204     1555   1555  2.26  
LINK         OD1 ASP A  93                CA    CA A 203     1555   1555  2.26  
LINK         OD1 ASP A  56                CA    CA A 201     1555   1555  2.28  
LINK         O   PHE A  99                CA    CA A 203     1555   1555  2.30  
LINK         O   THR A  26                CA    CA A 202     1555   1555  2.33  
LINK         OD1 ASP A  95                CA    CA A 203     1555   1555  2.34  
LINK         OD1 ASP A  24                CA    CA A 202     1555   1555  2.35  
LINK         O   GLN A 135                CA    CA A 204     1555   1555  2.37  
LINK         OD1 ASP A  58                CA    CA A 201     1555   1555  2.37  
LINK         OD1 ASN A  60                CA    CA A 201     1555   1555  2.38  
LINK         OD1 ASP A  22                CA    CA A 202     1555   1555  2.38  
LINK         OD1 ASP A  20                CA    CA A 202     1555   1555  2.38  
LINK         O   THR A  62                CA    CA A 201     1555   1555  2.42  
LINK         OD1 ASP A 133                CA    CA A 204     1555   1555  2.43  
LINK         OE1 GLU A 104                CA    CA A 203     1555   1555  2.48  
LINK         OE1 GLU A 140                CA    CA A 204     1555   1555  2.48  
LINK         OE1 GLU A  67                CA    CA A 201     1555   1555  2.49  
LINK         OD1 ASN A  97                CA    CA A 203     1555   1555  2.50  
LINK         OE2 GLU A 104                CA    CA A 203     1555   1555  2.51  
LINK         OE2 GLU A  31                CA    CA A 202     1555   1555  2.52  
LINK         OE1 GLU A  31                CA    CA A 202     1555   1555  2.56  
LINK         OE2 GLU A  67                CA    CA A 201     1555   1555  2.58  
LINK         OD1 ASP A 131                CA    CA A 204     1555   1555  2.58  
LINK         OE2 GLU A 140                CA    CA A 204     1555   1555  2.60  
SITE     1 AC1  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC1  5 GLU A  67                                                     
SITE     1 AC2  5 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC2  5 GLU A  31                                                     
SITE     1 AC3  5 ASP A  93  ASP A  95  ASN A  97  PHE A  99                    
SITE     2 AC3  5 GLU A 104                                                     
SITE     1 AC4  5 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  5 GLU A 140                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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