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Database: PDB
Entry: 2FXM
LinkDB: 2FXM
Original site: 2FXM 
HEADER    CONTRACTILE PROTEIN                     06-FEB-06   2FXM              
TITLE     STRUCTURE OF THE HUMAN BETA-MYOSIN S2 FRAGMENT                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN HEAVY CHAIN, CARDIAC MUSCLE BETA ISOFORM;           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DELTA-S2 FRAGMENT (838-963);                               
COMPND   5 SYNONYM: BETA-MYOSIN, MYHC-BETA;                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: HEART MUSCLE;                                                
SOURCE   6 GENE: HSBMHC;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    COILED COIL (DIMERIC, PARALLEL), FAMILIAL HYPERTROPHIC                
KEYWDS   2 CARDIOMYOPATHY, THICK FILAMENT, CONTRACTILE PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,N.H.THOMA,J.S.WRAY,M.GAUTEL,I.SCHLICHTING              
REVDAT   3   18-OCT-17 2FXM    1       REMARK                                   
REVDAT   2   24-FEB-09 2FXM    1       VERSN                                    
REVDAT   1   21-NOV-06 2FXM    0                                                
JRNL        AUTH   W.BLANKENFELDT,N.H.THOMA,J.S.WRAY,M.GAUTEL,I.SCHLICHTING     
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CARDIAC {BETA}-MYOSIN II         
JRNL        TITL 2 S2-{DELTA} PROVIDE INSIGHT INTO THE FUNCTIONAL ROLE OF THE   
JRNL        TITL 3 S2 SUBFRAGMENT                                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 17713 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17095604                                                     
JRNL        DOI    10.1073/PNAS.0606741103                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.GRUEN,M.GAUTEL                                             
REMARK   1  TITL   MUTATIONS IN BETA-MYOSIN S2 THAT CAUSE FAMILIAL HYPERTROPHIC 
REMARK   1  TITL 2 CARDIOMYOPATHY (FHC) ABOLISH THE INTERACTION WITH THE        
REMARK   1  TITL 3 REGULATORY DOMAIN OF MYOSIN-BINDING PROTEIN-C                
REMARK   1  REF    J.MOL.BIOL.                   V. 286   933 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   10024460                                                     
REMARK   1  DOI    10.1006/JMBI.1998.2522                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.LI,J.H.BROWN,L.RESHETNIKOVA,A.BLAZSEK,L.FARKAS,L.NYITRAY,  
REMARK   1  AUTH 2 C.COHEN                                                      
REMARK   1  TITL   VISUALIZATION OF AN UNSTABLE COILED COIL FROM THE SCALLOP    
REMARK   1  TITL 2 MYOSIN ROD                                                   
REMARK   1  REF    NATURE                        V. 424   341 2003              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   12867988                                                     
REMARK   1  DOI    10.1038/NATURE01801                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 9756                           
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) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 496                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 37                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1953                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -12.99500                                            
REMARK   3    B22 (A**2) : -32.36000                                            
REMARK   3    B33 (A**2) : 45.35400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.180                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TARGET SIGMA VALUES FOR RESTRAINED B      
REMARK   3  -FACTOR REFINEMENT HAVE BEEN RELAXED TO 10 A*A TO REFLECT THE       
REMARK   3  SPECIAL SHAPE OF THE MOLECULE. ATOMS THAT COULD NOT BE LOCATED      
REMARK   3  HAVE BEEN ASSIGNED A TEMPERATURE FACTOR OF 500 A*A AND OCCUPANCY    
REMARK   3  VALUE OF 0 FOR BETTER DISCERNABILITY.                               
REMARK   4                                                                      
REMARK   4 2FXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-FEB-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036431.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0088, 0.82655                    
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9756                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD, SHARP                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM CITRATE, TRIS- HCL,    
REMARK 280  PH 8.50, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      186.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      186.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       20.14500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       22.98500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       20.14500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       22.98500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      186.85000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       20.14500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       22.98500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      186.85000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       20.14500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       22.98500            
REMARK 290   SMTRY3   8  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: 6600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 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     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     PRO B   838                                                      
REMARK 465     LEU B   839                                                      
REMARK 465     LEU B   840                                                      
REMARK 465     LYS B   841                                                      
REMARK 465     SER B   842                                                      
REMARK 465     ALA B   843                                                      
REMARK 465     GLU B   844                                                      
REMARK 465     ARG B   845                                                      
REMARK 465     GLU B   846                                                      
REMARK 465     LYS B   847                                                      
REMARK 465     GLU B   848                                                      
REMARK 465     MET B   849                                                      
REMARK 465     ALA B   962                                                      
REMARK 465     LYS B   963                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     PRO A  838   CG   CD                                             
REMARK 480     GLU A  927   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  853   CG   CD   CE   NZ                                   
REMARK 480     LYS B  860   CG   CD   CE                                        
REMARK 480     GLU B  864   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  871   CG   CD   CE   NZ                                   
REMARK 480     LYS B  942   CD   CE   NZ                                        
REMARK 480     LEU B  959   CG   CD1  CD2                                       
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                              HG B   1  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 947   SG                                                     
REMARK 620 2 CYS B 947   SG  179.3                                              
REMARK 620 3 LEU B 943   O    89.4  90.8                                        
REMARK 620 4 CYS B 947   N   102.6  77.1  49.9                                  
REMARK 620 5 CYS A 947   N    69.2 110.7 154.0 147.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG A   2  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 905   SG                                                     
REMARK 620 2 CYS B 905   SG  179.9                                              
REMARK 620 3 ALA B 901   O    96.7  83.2                                        
REMARK 620 4 CYS A 905   N    69.8 110.3 161.8                                  
REMARK 620 5 ALA A 901   O    87.4  92.7 110.4  58.4                            
REMARK 620 6 CYS B 905   N   105.5  74.4  51.1 142.8 157.8                      
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 HG B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 2                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NKN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FXO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, E924K MUTANT                                       
DBREF  2FXM A  838   963  UNP    P12883   MYH7_HUMAN     838    963             
DBREF  2FXM B  838   963  UNP    P12883   MYH7_HUMAN     838    963             
SEQADV 2FXM GLY A   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXM SER A   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXM SER A   -1  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXM GLY B   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXM SER B   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXM SER B   -1  UNP  P12883              CLONING ARTIFACT               
SEQRES   1 A  129  GLY SER SER PRO LEU LEU LYS SER ALA GLU ARG GLU LYS          
SEQRES   2 A  129  GLU MET ALA SER MET LYS GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 A  129  GLU ALA LEU GLU LYS SER GLU ALA ARG ARG LYS GLU LEU          
SEQRES   4 A  129  GLU GLU LYS MET VAL SER LEU LEU GLN GLU LYS ASN ASP          
SEQRES   5 A  129  LEU GLN LEU GLN VAL GLN ALA GLU GLN ASP ASN LEU ALA          
SEQRES   6 A  129  ASP ALA GLU GLU ARG CYS ASP GLN LEU ILE LYS ASN LYS          
SEQRES   7 A  129  ILE GLN LEU GLU ALA LYS VAL LYS GLU MET ASN GLU ARG          
SEQRES   8 A  129  LEU GLU ASP GLU GLU GLU MET ASN ALA GLU LEU THR ALA          
SEQRES   9 A  129  LYS LYS ARG LYS LEU GLU ASP GLU CYS SER GLU LEU LYS          
SEQRES  10 A  129  ARG ASP ILE ASP ASP LEU GLU LEU THR LEU ALA LYS              
SEQRES   1 B  129  GLY SER SER PRO LEU LEU LYS SER ALA GLU ARG GLU LYS          
SEQRES   2 B  129  GLU MET ALA SER MET LYS GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 B  129  GLU ALA LEU GLU LYS SER GLU ALA ARG ARG LYS GLU LEU          
SEQRES   4 B  129  GLU GLU LYS MET VAL SER LEU LEU GLN GLU LYS ASN ASP          
SEQRES   5 B  129  LEU GLN LEU GLN VAL GLN ALA GLU GLN ASP ASN LEU ALA          
SEQRES   6 B  129  ASP ALA GLU GLU ARG CYS ASP GLN LEU ILE LYS ASN LYS          
SEQRES   7 B  129  ILE GLN LEU GLU ALA LYS VAL LYS GLU MET ASN GLU ARG          
SEQRES   8 B  129  LEU GLU ASP GLU GLU GLU MET ASN ALA GLU LEU THR ALA          
SEQRES   9 B  129  LYS LYS ARG LYS LEU GLU ASP GLU CYS SER GLU LEU LYS          
SEQRES  10 B  129  ARG ASP ILE ASP ASP LEU GLU LEU THR LEU ALA LYS              
HET     HG  A   2       1                                                       
HET     HG  B   1       1                                                       
HETNAM      HG MERCURY (II) ION                                                 
FORMUL   3   HG    2(HG 2+)                                                     
HELIX    1   1 LEU A  839  LYS A  963  1                                 125    
HELIX    2   2 SER B  851  LEU B  961  1                                 111    
LINK        HG    HG B   1                 SG  CYS A 947     1555   1555  2.32  
LINK        HG    HG B   1                 SG  CYS B 947     1555   1555  2.29  
LINK        HG    HG A   2                 SG  CYS A 905     1555   1555  2.30  
LINK        HG    HG A   2                 SG  CYS B 905     1555   1555  2.29  
LINK        HG    HG A   2                 O   ALA B 901     1555   1555  3.49  
LINK        HG    HG A   2                 N   CYS A 905     1555   1555  3.42  
LINK        HG    HG A   2                 O   ALA A 901     1555   1555  3.17  
LINK        HG    HG A   2                 N   CYS B 905     1555   1555  3.41  
LINK        HG    HG B   1                 O   LEU B 943     1555   1555  3.49  
LINK        HG    HG B   1                 N   CYS B 947     1555   1555  3.32  
LINK        HG    HG B   1                 N   CYS A 947     1555   1555  3.54  
SITE     1 AC1  4 LEU A 943  CYS A 947  LEU B 943  CYS B 947                    
SITE     1 AC2  4 ALA A 901  CYS A 905  ALA B 901  CYS B 905                    
CRYST1   40.290   45.970  373.700  90.00  90.00  90.00 C 2 2 21     16          
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      0.024820  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021753  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002676        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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