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Database: PDB
Entry: 2IX7
LinkDB: 2IX7
Original site: 2IX7 
HEADER    CONTRACTILE PROTEIN/METAL BINDING       07-JUL-06   2IX7              
TITLE     STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-146;                                            
COMPND   5 SYNONYM: CAM;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: APO-CALMODULIN;                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MYOSIN-5A;                                                 
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: RESIDUES 763-820;                                          
COMPND  12 SYNONYM: MYOSIN VA, DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE;           
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: IQ MOTIFS                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGP1-2;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    CONTRACTILE PROTEIN/METAL BINDING, ACTIN-BINDING, UBL CONJUGATION,    
KEYWDS   2 CA2+ REGULATION, MYOSIN, CALCIUM, IQ MOTIF, CALMODULIN, ACETYLATION, 
KEYWDS   3 NUCLEOTIDE- BINDING, CONTRACTILE PROTEIN, COMPLEX, PHOSPHORYLATION,  
KEYWDS   4 CALMODULIN-BINDING, METAL BINDING, METHYLATION, COILED COIL, ATP-    
KEYWDS   5 BINDING, MOTOR PROTEIN, CONTRACTILE PROTEIN-METAL BINDING COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HOUDUSSE,J.F.GAUCHER,S.MUI,E.KREMENTSOVA,K.M.TRYBUS,C.COHEN         
REVDAT   7   13-DEC-23 2IX7    1       REMARK                                   
REVDAT   6   08-NOV-23 2IX7    1       REMARK SSBOND LINK                       
REVDAT   5   27-FEB-19 2IX7    1       REMARK LINK                              
REVDAT   4   04-DEC-13 2IX7    1       SOURCE REMARK VERSN  FORMUL              
REVDAT   3   24-FEB-09 2IX7    1       VERSN                                    
REVDAT   2   02-JAN-07 2IX7    1       JRNL                                     
REVDAT   1   13-DEC-06 2IX7    0                                                
JRNL        AUTH   A.HOUDUSSE,J.F.GAUCHER,E.KREMENTSOVA,S.MUI,K.M.TRYBUS,       
JRNL        AUTH 2 C.COHEN                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF APO-CALMODULIN BOUND TO THE FIRST TWO   
JRNL        TITL 2 IQ MOTIFS OF MYOSIN V REVEALS ESSENTIAL RECOGNITION          
JRNL        TITL 3 FEATURES.                                                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 19326 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17151196                                                     
JRNL        DOI    10.1073/PNAS.0609436103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3356211.510                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25977                          
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 SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2570                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3860                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 430                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2759                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.34000                                              
REMARK   3    B22 (A**2) : 5.34000                                              
REMARK   3    B33 (A**2) : -10.69000                                            
REMARK   3    B12 (A**2) : 3.99000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.850                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.080 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.590 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.580 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.490 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 57.09                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED. THE STRUCTURE    
REMARK   3  WAS FIRST SOLVED BY MIRAS AND THEN REFINED WITH A NON               
REMARK   3  ISOMORPHOUS NATIVE DATA SET.                                        
REMARK   4                                                                      
REMARK   4 2IX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029284.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9134                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25837                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1WCD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION METHOD (4 C) PROTEIN     
REMARK 280  SOLUTION; 10MG/ML IN 10MM IMIDAZOL PH7.0, 20MM NACL. RESERVOIR;     
REMARK 280  1.8M SA, 50MM MES PH5.0, 5% MPD, 5MM EGTA, 2MM NAN3, PH 5.00,       
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.22667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.11333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.11333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       68.22667            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 6660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 B1148  LIES ON A SPECIAL POSITION.                          
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     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     ASP B 133    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  21      -34.54    -39.61                                   
REMARK 500    ASN A  42       74.19   -113.43                                   
REMARK 500    GLU A  54       25.44    -73.60                                   
REMARK 500    VAL A  55      -23.90   -159.77                                   
REMARK 500    ASP A  56       45.96   -109.70                                   
REMARK 500    ASP A  93       78.21   -107.28                                   
REMARK 500    LYS A  94      -76.13    -25.20                                   
REMARK 500    LYS A 115      118.08    -27.41                                   
REMARK 500    ARG B  74      -67.69    -91.23                                   
REMARK 500    ASP B  78       46.86   -155.54                                   
REMARK 500    ASP B  80      172.31    -59.70                                   
REMARK 500    SER B  81      156.30    178.23                                   
REMARK 500    ASN B 111      -39.86   -131.85                                   
REMARK 500    ASP C 764      158.13    177.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1147                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1148                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1149                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1257                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1258                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS C 1259                
DBREF  2IX7 A    2   146  UNP    P62204   CALM_MOUSE       2    146             
DBREF  2IX7 B    2   146  UNP    P62204   CALM_MOUSE       2    146             
DBREF  2IX7 C  763   820  UNP    Q99104   MYO5A_MOUSE    763    820             
SEQRES   1 A  145  ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU          
SEQRES   2 A  145  ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE          
SEQRES   3 A  145  THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY          
SEQRES   4 A  145  GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN          
SEQRES   5 A  145  GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO          
SEQRES   6 A  145  GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR          
SEQRES   7 A  145  ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE          
SEQRES   8 A  145  ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU          
SEQRES   9 A  145  ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP          
SEQRES  10 A  145  GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP          
SEQRES  11 A  145  GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET          
SEQRES  12 A  145  MET THR                                                      
SEQRES   1 B  145  ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU          
SEQRES   2 B  145  ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE          
SEQRES   3 B  145  THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY          
SEQRES   4 B  145  GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN          
SEQRES   5 B  145  GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO          
SEQRES   6 B  145  GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR          
SEQRES   7 B  145  ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE          
SEQRES   8 B  145  ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU          
SEQRES   9 B  145  ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP          
SEQRES  10 B  145  GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP          
SEQRES  11 B  145  GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET          
SEQRES  12 B  145  MET THR                                                      
SEQRES   1 C   58  ALA ASP LYS LEU ARG ALA ALA CYS ILE ARG ILE GLN LYS          
SEQRES   2 C   58  THR ILE ARG GLY TRP LEU LEU ARG LYS ARG TYR LEU CYS          
SEQRES   3 C   58  MET GLN ARG ALA ALA ILE THR VAL GLN ARG TYR VAL ARG          
SEQRES   4 C   58  GLY TYR GLN ALA ARG CYS TYR ALA LYS PHE LEU ARG ARG          
SEQRES   5 C   58  THR LYS ALA ALA THR THR                                      
HET    SO4  B1147       5                                                       
HET    SO4  B1148       5                                                       
HET    SO4  B1149       5                                                       
HET    CYS  C1259       7                                                       
HET    SO4  C1257       5                                                       
HET    SO4  C1258       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CYS CYSTEINE                                                         
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   7  CYS    C3 H7 N O2 S                                                 
FORMUL  10  HOH   *144(H2 O)                                                    
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 GLU A   31  LEU A   39  1                                   9    
HELIX    3   3 THR A   44  GLU A   54  1                                  11    
HELIX    4   4 PHE A   65  ASP A   78  1                                  14    
HELIX    5   5 SER A   81  VAL A   91  1                                  11    
HELIX    6   6 ALA A  102  LEU A  112  1                                  11    
HELIX    7   7 THR A  117  ALA A  128  1                                  12    
HELIX    8   8 ASN A  137  MET A  145  1                                   9    
HELIX    9   9 THR B    5  PHE B   19  1                                  15    
HELIX   10  10 GLU B   31  LEU B   39  1                                   9    
HELIX   11  11 THR B   44  VAL B   55  1                                  12    
HELIX   12  12 PHE B   65  MET B   76  1                                  12    
HELIX   13  13 SER B   81  VAL B   91  1                                  11    
HELIX   14  14 ALA B  102  THR B  110  1                                   9    
HELIX   15  15 THR B  117  GLU B  127  1                                  11    
HELIX   16  16 TYR B  138  THR B  146  1                                   9    
HELIX   17  17 ASP C  764  THR C  819  1                                  56    
SHEET    1  AA 2 THR A  26  THR A  28  0                                        
SHEET    2  AA 2 THR A  62  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1  AB 2 ILE A 100  SER A 101  0                                        
SHEET    2  AB 2 GLN A 135  VAL A 136 -1  N  VAL A 136   O  ILE A 100           
SHEET    1  BA 2 THR B  26  THR B  28  0                                        
SHEET    2  BA 2 THR B  62  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
SHEET    1  BB 2 TYR B  99  SER B 101  0                                        
SHEET    2  BB 2 GLN B 135  ASN B 137 -1  O  VAL B 136   N  ILE B 100           
SSBOND   1 CYS C  788    CYS C 1259                          1555   1555  2.04  
SITE     1 AC1  5 GLY B  61  THR B  62  HOH B2051  ASP C 764                    
SITE     2 AC1  5 LYS C 765                                                     
SITE     1 AC2  2 ASP B 131  GLY B 132                                          
SITE     1 AC3  4 ARG B 106  HIS B 107  THR B 110  HOH B2082                    
SITE     1 AC4  3 LYS C 810  ARG C 813  HOH C2030                               
SITE     1 AC5  1 ARG C 814                                                     
SITE     1 AC6  2 CYS C 788  ARG C 791                                          
CRYST1  112.000  112.000  102.340  90.00  90.00 120.00 P 32 2 1     12          
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      0.008929  0.005155  0.000000        0.00000                         
SCALE2      0.000000  0.010310  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009771        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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