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Database: PDB
Entry: 2FXO
LinkDB: 2FXO
Original site: 2FXO 
HEADER    CONTRACTILE PROTEIN                     06-FEB-06   2FXO              
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, C, D;                                                   
COMPND   4 FRAGMENT: DELTA-S2 FRAGMENT (838-963);                               
COMPND   5 SYNONYM: BETA-MYOSIN, MYHC-BETA;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: 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, FHC-ASSOCIATED MUTANT E924K, THICK FILAMENT,         
KEYWDS   3 CONTRACTILE PROTEIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,N.H.THOMA,J.S.WRAY,M.GAUTEL,I.SCHLICHTING              
REVDAT   4   18-OCT-17 2FXO    1       REMARK                                   
REVDAT   3   13-JUL-11 2FXO    1       VERSN                                    
REVDAT   2   24-FEB-09 2FXO    1       VERSN                                    
REVDAT   1   21-NOV-06 2FXO    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19157                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.277                           
REMARK   3   R VALUE            (WORKING SET) : 0.273                           
REMARK   3   FREE R VALUE                     : 0.349                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1040                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1396                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.5110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4145                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 61.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.30000                                             
REMARK   3    B22 (A**2) : 0.74000                                              
REMARK   3    B33 (A**2) : 1.76000                                              
REMARK   3    B12 (A**2) : 1.34000                                              
REMARK   3    B13 (A**2) : -5.88000                                             
REMARK   3    B23 (A**2) : -0.69000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.891         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.419         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.458         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.647        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4151 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3874 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5508 ; 1.526 ; 2.019       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9178 ; 3.650 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   504 ; 6.104 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   619 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4472 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   648 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   914 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3836 ; 0.259 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2490 ; 0.104 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    57 ; 0.192 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.189 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    68 ; 0.286 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.131 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2539 ; 6.269 ;10.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4054 ; 8.380 ;10.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1612 ; 6.774 ;10.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1454 ; 9.684 ;10.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A   963                          
REMARK   3    RESIDUE RANGE :   B    -1        B   961                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8110  -1.1590  -2.5750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1368 T22:   0.0196                                     
REMARK   3      T33:   0.1116 T12:  -0.0054                                     
REMARK   3      T13:   0.1098 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0365 L22:   0.2889                                     
REMARK   3      L33:   2.3626 L12:   1.2256                                     
REMARK   3      L13:   3.7589 L23:   0.8388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0751 S12:  -0.0033 S13:  -0.1861                       
REMARK   3      S21:  -0.0104 S22:  -0.0372 S23:  -0.0309                       
REMARK   3      S31:   0.0352 S32:  -0.0052 S33:  -0.0379                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -2        C   962                          
REMARK   3    RESIDUE RANGE :   D    -1        D   963                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.7230  10.0250 -25.6260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1523 T22:   0.0694                                     
REMARK   3      T33:   0.1116 T12:  -0.0038                                     
REMARK   3      T13:   0.0784 T23:   0.0438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9035 L22:   0.3286                                     
REMARK   3      L33:   2.9717 L12:   1.3851                                     
REMARK   3      L13:   4.2585 L23:   1.0037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0265 S12:   0.2158 S13:   0.2185                       
REMARK   3      S21:   0.0059 S22:  -0.0620 S23:   0.0235                       
REMARK   3      S31:  -0.0043 S32:   0.1017 S33:   0.0885                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. TARGET SIGMA VALUES FOR RESTRAINED B-FACTOR              
REMARK   3  REFINEMENT HAVE BEEN RELAXED TO 10 A*A TO REFLECT THE SPECIAL       
REMARK   3  SHAPE OF THE MOLECULE. ATOMS THAT COULD NOT BE LOCATED HAVE BEEN    
REMARK   3  ASSIGNED A TEMPERATURE FACTOR OF 500 A*A AND OCCUPANCY VALUE OF     
REMARK   3  0 FOR BETTER DISCERNABILITY.                                        
REMARK   4                                                                      
REMARK   4 2FXO 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_1000036432.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20190                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
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) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD WITH SEMI-BRUTE- FORCE   
REMARK 200  MOLECULAR REPLACEMENT                                               
REMARK 200 SOFTWARE USED: SHELXD, MOLEMAN2                                      
REMARK 200 STARTING MODEL: PDB ENTRY 1XNM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM ACETATE, TRIS-HCL, PH   
REMARK 280  7.50, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 6890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 6840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ALA B   962                                                      
REMARK 465     LYS B   963                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     LYS C   963                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
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     LYS A  847   CG   CD   CE   NZ                                   
REMARK 480     LYS A  871   CG   CD   CE   NZ                                   
REMARK 480     GLU A  872   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  876   CE   NZ                                             
REMARK 480     LYS A  924   CD   CE   NZ                                        
REMARK 480     LEU B  840   CG   CD1  CD2                                       
REMARK 480     LYS B  847   CG   CD   CE   NZ                                   
REMARK 480     GLU B  854   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  865   CE   NZ                                             
REMARK 480     LEU B  961   CG   CD1  CD2                                       
REMARK 480     LYS C  942   CG   CD   CE   NZ                                   
REMARK 480     SER D   -1   OG                                                  
REMARK 480     LEU D  839   CG   CD1  CD2                                       
REMARK 480     LYS D  841   CE   NZ                                             
REMARK 480     GLU D  872   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  876   CG   CD   CE   NZ                                   
REMARK 480     GLN D  882   CG   CD   OE1  NE2                                  
REMARK 480     LEU D  889   CD1  CD2                                            
REMARK 480     GLU D  903   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  910   CG   CD   CE   NZ                                   
REMARK 480     GLN D  914   CG   CD   OE1  NE2                                  
REMARK 480     GLU D  931   CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN B   907     NZ   LYS D   865              2.13            
REMARK 500   ND2  ASN A   933     OD1  ASN B   933              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP C 906   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP D 953   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 955   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
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    PRO A 838      -19.31    -42.55                                   
REMARK 500    LYS B 841      -16.90    -49.43                                   
REMARK 500    ALA D 962      135.39    -24.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FXM   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, WILD TYPE                                          
REMARK 900 RELATED ID: 1NKN   RELATED DB: PDB                                   
DBREF  2FXO A  838   963  UNP    P12883   MYH7_HUMAN     838    963             
DBREF  2FXO B  838   963  UNP    P12883   MYH7_HUMAN     838    963             
DBREF  2FXO C  838   963  UNP    P12883   MYH7_HUMAN     838    963             
DBREF  2FXO D  838   963  UNP    P12883   MYH7_HUMAN     838    963             
SEQADV 2FXO GLY A   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER A   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER A   -1  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO LYS A  924  UNP  P12883    GLU   924 ENGINEERED                     
SEQADV 2FXO GLY B   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER B   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER B   -1  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO LYS B  924  UNP  P12883    GLU   924 ENGINEERED                     
SEQADV 2FXO GLY C   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER C   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER C   -1  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO LYS C  924  UNP  P12883    GLU   924 ENGINEERED                     
SEQADV 2FXO GLY D   -3  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER D   -2  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO SER D   -1  UNP  P12883              CLONING ARTIFACT               
SEQADV 2FXO LYS D  924  UNP  P12883    GLU   924 ENGINEERED                     
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 LYS 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 LYS 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              
SEQRES   1 C  129  GLY SER SER PRO LEU LEU LYS SER ALA GLU ARG GLU LYS          
SEQRES   2 C  129  GLU MET ALA SER MET LYS GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 C  129  GLU ALA LEU GLU LYS SER GLU ALA ARG ARG LYS GLU LEU          
SEQRES   4 C  129  GLU GLU LYS MET VAL SER LEU LEU GLN GLU LYS ASN ASP          
SEQRES   5 C  129  LEU GLN LEU GLN VAL GLN ALA GLU GLN ASP ASN LEU ALA          
SEQRES   6 C  129  ASP ALA GLU GLU ARG CYS ASP GLN LEU ILE LYS ASN LYS          
SEQRES   7 C  129  ILE GLN LEU GLU ALA LYS VAL LYS GLU MET ASN LYS ARG          
SEQRES   8 C  129  LEU GLU ASP GLU GLU GLU MET ASN ALA GLU LEU THR ALA          
SEQRES   9 C  129  LYS LYS ARG LYS LEU GLU ASP GLU CYS SER GLU LEU LYS          
SEQRES  10 C  129  ARG ASP ILE ASP ASP LEU GLU LEU THR LEU ALA LYS              
SEQRES   1 D  129  GLY SER SER PRO LEU LEU LYS SER ALA GLU ARG GLU LYS          
SEQRES   2 D  129  GLU MET ALA SER MET LYS GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 D  129  GLU ALA LEU GLU LYS SER GLU ALA ARG ARG LYS GLU LEU          
SEQRES   4 D  129  GLU GLU LYS MET VAL SER LEU LEU GLN GLU LYS ASN ASP          
SEQRES   5 D  129  LEU GLN LEU GLN VAL GLN ALA GLU GLN ASP ASN LEU ALA          
SEQRES   6 D  129  ASP ALA GLU GLU ARG CYS ASP GLN LEU ILE LYS ASN LYS          
SEQRES   7 D  129  ILE GLN LEU GLU ALA LYS VAL LYS GLU MET ASN LYS ARG          
SEQRES   8 D  129  LEU GLU ASP GLU GLU GLU MET ASN ALA GLU LEU THR ALA          
SEQRES   9 D  129  LYS LYS ARG LYS LEU GLU ASP GLU CYS SER GLU LEU LYS          
SEQRES  10 D  129  ARG ASP ILE ASP ASP LEU GLU LEU THR LEU ALA LYS              
HELIX    1   1 SER A   -2  LEU A  959  1                                 124    
HELIX    2   2 SER B  842  LYS B  847  1                                   6    
HELIX    3   3 LYS B  847  THR B  960  1                                 114    
HELIX    4   4 SER C   -2  LEU C  959  1                                 124    
HELIX    5   5 SER D   -1  GLN D  907  1                                  71    
HELIX    6   6 GLN D  907  THR D  960  1                                  54    
SSBOND   1 CYS A  947    CYS B  947                          1555   1555  2.11  
SSBOND   2 CYS C  947    CYS D  947                          1555   1555  2.12  
CRYST1   40.157   41.867   97.795  91.11  92.73 107.18 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024902  0.007699  0.001458        0.00000                         
SCALE2      0.000000  0.025001  0.000877        0.00000                         
SCALE3      0.000000  0.000000  0.010243        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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