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Database: PDB
Entry: 2Y8I
LinkDB: 2Y8I
Original site: 2Y8I 
HEADER    MOTOR PROTEIN                           07-FEB-11   2Y8I              
TITLE     STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION BY
TITLE    2 MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN-2 HEAVY CHAIN;                                      
COMPND   3 CHAIN: X;                                                            
COMPND   4 FRAGMENT: MOTOR DOMAIN, RESIDUES 2-759;                              
COMPND   5 SYNONYM: MYOSIN II HEAVY CHAIN;                                      
COMPND   6 EC: 3.6.4.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;                       
SOURCE   3 ORGANISM_COMMON: SLIME MOLD;                                         
SOURCE   4 ORGANISM_TAXID: 44689;                                               
SOURCE   5 EXPRESSION_SYSTEM: DICTYOSTELIUM DISCOIDEUM;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 44689;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PDXA-3H                                    
KEYWDS    MOTOR PROTEIN, ADP COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PRELLER,S.BAUER,N.ADAMEK,S.FUJITA-BECKER,R.FEDOROV,M.A.GEEVES,      
AUTHOR   2 D.J.MANSTEIN                                                         
REVDAT   5   20-DEC-23 2Y8I    1       REMARK                                   
REVDAT   4   31-JUL-19 2Y8I    1       REMARK LINK                              
REVDAT   3   20-JUN-18 2Y8I    1       REMARK                                   
REVDAT   2   12-OCT-11 2Y8I    1       JRNL                                     
REVDAT   1   20-JUL-11 2Y8I    0                                                
JRNL        AUTH   M.PRELLER,S.BAUER,N.ADAMEK,S.FUJITA-BECKER,R.FEDOROV,        
JRNL        AUTH 2 M.A.GEEVES,D.J.MANSTEIN                                      
JRNL        TITL   STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN   
JRNL        TITL 2 FUNCTION BY REACTIVE THIOL REGION MUTATIONS G680A AND G680V. 
JRNL        REF    J.BIOL.CHEM.                  V. 286 35051 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21841195                                                     
JRNL        DOI    10.1074/JBC.M111.265298                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18481                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.337                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 942                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 20.2159 -  5.9481    1.00     2761   131  0.2955 0.3863        
REMARK   3     2  5.9481 -  4.7413    1.00     2618   148  0.2329 0.2760        
REMARK   3     3  4.7413 -  4.1478    1.00     2595   140  0.1876 0.3040        
REMARK   3     4  4.1478 -  3.7713    1.00     2552   159  0.2216 0.3100        
REMARK   3     5  3.7713 -  3.5025    1.00     2559   143  0.2298 0.3738        
REMARK   3     6  3.5025 -  3.2969    1.00     2563   130  0.2574 0.3580        
REMARK   3     7  3.2969 -  3.1324    0.83     1891    91  0.2904 0.3800        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.40                                          
REMARK   3   SHRINKAGE RADIUS   : 1.17                                          
REMARK   3   K_SOL              : 0.15                                          
REMARK   3   B_SOL              : 30.70                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.560            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.07140                                             
REMARK   3    B22 (A**2) : -9.77290                                             
REMARK   3    B33 (A**2) : -3.98930                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           6237                                  
REMARK   3   ANGLE     :  1.360           8428                                  
REMARK   3   CHIRALITY :  0.089            918                                  
REMARK   3   PLANARITY :  0.004           1104                                  
REMARK   3   DIHEDRAL  : 23.988           2338                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Y8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290046913.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9175                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20093                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1MMD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 6000, 4% GLYCEROL., PH 7.0       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.25000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       90.25000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN X, GLY 680 TO ALA                        
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     ASN X   206                                                      
REMARK 475     GLY X   207                                                      
REMARK 475     SER X   208                                                      
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   O    HOH X  2239     O    HOH X  2240              0.53            
REMARK 500   O    HOH X  2237     O    HOH X  2238              0.60            
REMARK 500   O    LYS X   554     O    HOH X  2183              1.32            
REMARK 500   CE1  PHE X   225     CD1  ILE X   280              1.36            
REMARK 500   O    ASN X   376     OG1  THR X   380              1.39            
REMARK 500   ND2  ASN X   203     O    ALA X   205              1.41            
REMARK 500   O    ARG X   689     N    GLY X   691              1.42            
REMARK 500   O    ASN X   219     OE1  GLU X   223              1.54            
REMARK 500   O    LEU X   222     O    HOH X  2082              1.55            
REMARK 500   O    GLN X   593     O    HOH X  2193              1.65            
REMARK 500   C    LEU X   222     O    HOH X  2082              1.65            
REMARK 500   ND2  ASN X   679     O    HOH X  2214              1.78            
REMARK 500   O    PHE X    85     CG1  VAL X    88              1.82            
REMARK 500   C    PHE X    85     O    HOH X  2039              1.84            
REMARK 500   ND2  ASN X   172     CD2  PHE X   449              1.84            
REMARK 500   C    LYS X   703     O    HOH X  2219              1.89            
REMARK 500   O    THR X    64     N    GLY X    67              1.91            
REMARK 500   C    LEU X   121     O    HOH X  2048              1.92            
REMARK 500   O    GLN X   213     O    HOH X  2079              1.94            
REMARK 500   OG   SER X   257     O    HOH X  2095              1.95            
REMARK 500   O    ALA X   748     O    HOH X  2251              1.95            
REMARK 500   OD1  ASN X   172     CA   TYR X   448              1.96            
REMARK 500   CA   ASP X    58     O    HOH X  2029              1.96            
REMARK 500   O    SER X   640     OG1  THR X   644              1.96            
REMARK 500   O    ILE X   514     OD1  ASP X   518              1.96            
REMARK 500   OG1  THR X   648     O    HOH X  2207              1.97            
REMARK 500   CG2  THR X   117     O    HOH X  2046              1.97            
REMARK 500   CB   PHE X   746     O    HOH X  2248              1.98            
REMARK 500   CD1  PHE X   692     O    HOH X  2243              1.98            
REMARK 500   CG   ASN X   172     O    HOH X  2067              1.99            
REMARK 500   CB   ASP X    40     O    HOH X  2022              2.00            
REMARK 500   N    GLY X    87     OD1  ASN X   105              2.00            
REMARK 500   CD1  TRP X   432     NZ   LYS X   610              2.00            
REMARK 500   OD2  ASP X   141     O    HOH X  2053              2.00            
REMARK 500   O    THR X   380     O    HOH X  2132              2.01            
REMARK 500   NH2  ARG X   170     O    HOH X  2063              2.02            
REMARK 500   C    GLU X   360     O    HOH X  2127              2.03            
REMARK 500   C    ASP X    58     O    HOH X  2029              2.04            
REMARK 500   O    ASN X   541     OG1  THR X   545              2.04            
REMARK 500   O    VAL X   702     CD2  TYR X   706              2.04            
REMARK 500   O    HOH X  2216     O    HOH X  2217              2.05            
REMARK 500   CG   ASN X   203     O    ALA X   205              2.06            
REMARK 500   CB   GLN X   213     O    HOH X  2078              2.06            
REMARK 500   OD1  ASN X   172     N    PHE X   449              2.06            
REMARK 500   CG   PHE X   692     O    HOH X  2243              2.06            
REMARK 500   O    GLU X   360     O    HOH X  2127              2.06            
REMARK 500   N    ASP X    58     O    HOH X  2029              2.06            
REMARK 500   C    LYS X   372     O    HOH X  2129              2.06            
REMARK 500   C    ASN X   219     OE1  GLU X   223              2.07            
REMARK 500   O    HOH X  2076     O    HOH X  2077              2.07            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      96 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG X   397     O    ARG X   402     2556     1.10            
REMARK 500   O    GLN X   204     OE2  GLU X   273     1455     1.56            
REMARK 500   CG   ARG X   402     O    HOH X  2255     3645     1.93            
REMARK 500   O    HOH X  2065     O    HOH X  2149     1455     2.02            
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    THR X  28   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES          
REMARK 500    PRO X  39   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    GLU X  55   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ASP X  58   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ASN X  78   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    GLY X 120   N   -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    GLY X 251   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    SER X 343   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    GLY X 364   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    VAL X 534   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    GLN X 594   N   -  CA  -  C   ANGL. DEV. =  19.1 DEGREES          
REMARK 500    ILE X 617   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    GLU X 683   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    TYR X 698   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    TYR X 705   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    TYR X 705   N   -  CA  -  C   ANGL. DEV. =  22.6 DEGREES          
REMARK 500    TYR X 706   N   -  CA  -  CB  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASN X 731   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    GLY X 749   N   -  CA  -  C   ANGL. DEV. =  16.4 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    SER X   9      113.69    -35.90                                   
REMARK 500    ASP X  10      -34.36    -36.83                                   
REMARK 500    VAL X  17        3.45    -67.34                                   
REMARK 500    LYS X  18       66.46     68.41                                   
REMARK 500    LEU X  27     -102.58   -150.44                                   
REMARK 500    PRO X  41        7.79    -61.47                                   
REMARK 500    LYS X  42      -90.42   -118.93                                   
REMARK 500    SER X  46       76.64    108.81                                   
REMARK 500    SER X  54      114.47   -166.61                                   
REMARK 500    LYS X  63       71.17   -166.97                                   
REMARK 500    ASP X  86      131.24    -32.10                                   
REMARK 500    ALA X 101       -6.43    -59.89                                   
REMARK 500    ASP X 113       11.27     82.79                                   
REMARK 500    PHE X 129      -12.52     81.79                                   
REMARK 500    PHE X 143        5.48    -61.52                                   
REMARK 500    ALA X 183      -12.89    -47.83                                   
REMARK 500    VAL X 210      -59.28   -138.61                                   
REMARK 500    ASN X 235       52.87   -118.69                                   
REMARK 500    PHE X 239     -159.81   -130.79                                   
REMARK 500    SER X 254      -86.09   -116.84                                   
REMARK 500    GLN X 283      -52.72   -132.48                                   
REMARK 500    LEU X 296       70.33   -154.25                                   
REMARK 500    HIS X 297      113.68      9.81                                   
REMARK 500    PRO X 301       69.52    -67.15                                   
REMARK 500    GLU X 302      -20.65   -168.05                                   
REMARK 500    VAL X 313      -68.26   -139.62                                   
REMARK 500    ASN X 376       -7.27    -52.31                                   
REMARK 500    VAL X 411      -16.02    -45.82                                   
REMARK 500    LEU X 421       -9.43    -57.57                                   
REMARK 500    TYR X 448      167.26     31.04                                   
REMARK 500    ILE X 450       78.41   -119.99                                   
REMARK 500    SER X 465      171.30    -57.71                                   
REMARK 500    GLU X 467      -33.22    -39.36                                   
REMARK 500    LYS X 498       10.34     80.85                                   
REMARK 500    TRP X 501      173.51    -56.82                                   
REMARK 500    PHE X 503      122.05    -31.21                                   
REMARK 500    PHE X 506      -62.99   -142.29                                   
REMARK 500    LEU X 508      104.96     69.61                                   
REMARK 500    ASP X 530        0.38    -69.28                                   
REMARK 500    ASP X 540      -73.43     -4.75                                   
REMARK 500    LEU X 547        1.93    -65.55                                   
REMARK 500    GLU X 559       96.70   -160.12                                   
REMARK 500    PHE X 563      -63.12   -126.48                                   
REMARK 500    TYR X 573       -0.78    -56.33                                   
REMARK 500    LEU X 592      133.81   -173.97                                   
REMARK 500    PRO X 615       -8.34    -48.83                                   
REMARK 500    ARG X 620     -162.72   -115.60                                   
REMARK 500    LYS X 623      -84.07   -179.28                                   
REMARK 500    ALA X 625       -6.26    170.01                                   
REMARK 500    GLU X 646        9.63    -66.33                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR X 186   OG1                                                    
REMARK 620 2 SER X 237   OG  134.3                                              
REMARK 620 3 ASP X 454   OD2  99.4 126.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP X 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 1002                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MNE   RELATED DB: PDB                                   
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED     
REMARK 900 WITH MG-PYROPHOSPHATE                                                
REMARK 900 RELATED ID: 1D1C   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH N-  
REMARK 900 METHYL-O-NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.    
REMARK 900 RELATED ID: 1W9L   RELATED DB: PDB                                   
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456E BOUND WITH     
REMARK 900 MGADP-ALF4                                                           
REMARK 900 RELATED ID: 1VOM   RELATED DB: PDB                                   
REMARK 900 COMPLEX BETWEEN DICTYOSTELIUM MYOSIN AND MGADP AND VANADATE AT 1.9A  
REMARK 900 RESOLUTION                                                           
REMARK 900 RELATED ID: 1MMN   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES   
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN                  
REMARK 900 RELATED ID: 2AKA   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE NUCLEOTIDE-FREE MYOSIN II MOTOR DOMAINFROM          
REMARK 900 DICTYOSTELIUM DISCOIDEUM FUSED TO THE GTPASE DOMAINOF DYNAMIN 1      
REMARK 900 FROM RATTUS NORVEGICUS                                               
REMARK 900 RELATED ID: 2JHR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 MOTOR DOMAIN IN COMPLEX WITH ADP-      
REMARK 900 METAVANADATE AND PENTABROMOPSEUDILIN                                 
REMARK 900 RELATED ID: 1W9J   RELATED DB: PDB                                   
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456Y BOUND WITH     
REMARK 900 MGADP-ALF4                                                           
REMARK 900 RELATED ID: 2X9H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 MOTOR DOMAIN IN COMPLEX WITH ADP-      
REMARK 900 METAVANADATE AND PENTACHLOROCARBAZOLE                                
REMARK 900 RELATED ID: 1FMV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE APO MOTOR DOMAIN OF DICTYOSTELLIUMMYOSIN II 
REMARK 900 RELATED ID: 1MMA   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES   
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN                  
REMARK 900 RELATED ID: 2XO8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 IN COMPLEX WITH                        
REMARK 900 TRIBROMODICHLOROPSEUDILIN                                            
REMARK 900 RELATED ID: 1MMG   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES   
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN                  
REMARK 900 RELATED ID: 1W9I   RELATED DB: PDB                                   
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456Y BOUND WITH     
REMARK 900 MGADP-BEFX                                                           
REMARK 900 RELATED ID: 1W9K   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM DISCOIDEUM MYOSIN II MOTOR DOMAIN S456E WITH BOUND     
REMARK 900 MGADP-BEFX                                                           
REMARK 900 RELATED ID: 1MND   RELATED DB: PDB                                   
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED     
REMARK 900 WITH MGADP-ALF4                                                      
REMARK 900 RELATED ID: 1JX2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASEDOMAIN,     
REMARK 900 DETERMINED AS MYOSIN FUSION                                          
REMARK 900 RELATED ID: 1Q5G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE NUCLEOTIDE-FREE MYOSIN II MOTOR DOMAINFROM          
REMARK 900 DICTYOSTELIUM DISCOIDEUM                                             
REMARK 900 RELATED ID: 1D0Y   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O-  
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM FLUORIDE.                
REMARK 900 RELATED ID: 2XEL   RELATED DB: PDB                                   
REMARK 900 MOLECULAR MECHANISM OF PENTACHLOROPSEUDILIN MEDIATED INHIBITION OF   
REMARK 900 MYOSIN MOTOR ACTIVITY                                                
REMARK 900 RELATED ID: 2JJ9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 IN COMPLEX WITH ADP- METAVANADATE      
REMARK 900 RELATED ID: 1LVK   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O -(N-                
REMARK 900 METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM     
REMARK 900 MYOSIN MOTOR DOMAIN                                                  
REMARK 900 RELATED ID: 1JWY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DYNAMIN A GTPASE DOMAIN COMPLEXEDWITH GDP,  
REMARK 900 DETERMINED AS MYOSIN FUSION                                          
REMARK 900 RELATED ID: 1YV3   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURAL BASIS OF BLEBBISTATIN INHIBITION ANDSPECIFICITY FOR   
REMARK 900 MYOSIN II                                                            
REMARK 900 RELATED ID: 1FMW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAINOF        
REMARK 900 DICTYOSTELIUM MYOSIN II                                              
REMARK 900 RELATED ID: 1D0X   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH M-  
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.             
REMARK 900 RELATED ID: 1D1B   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,  
REMARK 900 P-DINITROPHENYL AMINOPROPYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.        
REMARK 900 RELATED ID: 1G8X   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR                
REMARK 900 RELATED ID: 1D1A   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,  
REMARK 900 P-DINITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.         
REMARK 900 RELATED ID: 1D0Z   RELATED DB: PDB                                   
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH P-  
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.             
REMARK 900 RELATED ID: 1MMD   RELATED DB: PDB                                   
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED     
REMARK 900 WITH MGADP-BEF3                                                      
REMARK 900 RELATED ID: 2Y0R   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION  
REMARK 900 BY MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2                 
REMARK 900 RELATED ID: 2Y9E   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION  
REMARK 900 BY MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2                 
DBREF  2Y8I X    2   759  UNP    P08799   MYS2_DICDI       2    759             
SEQADV 2Y8I ALA X  680  UNP  P08799    GLY   680 ENGINEERED MUTATION            
SEQRES   1 X  758  ASN PRO ILE HIS ASP ARG THR SER ASP TYR HIS LYS TYR          
SEQRES   2 X  758  LEU LYS VAL LYS GLN GLY ASP SER ASP LEU PHE LYS LEU          
SEQRES   3 X  758  THR VAL SER ASP LYS ARG TYR ILE TRP TYR ASN PRO ASP          
SEQRES   4 X  758  PRO LYS GLU ARG ASP SER TYR GLU CYS GLY GLU ILE VAL          
SEQRES   5 X  758  SER GLU THR SER ASP SER PHE THR PHE LYS THR VAL ASP          
SEQRES   6 X  758  GLY GLN ASP ARG GLN VAL LYS LYS ASP ASP ALA ASN GLN          
SEQRES   7 X  758  ARG ASN PRO ILE LYS PHE ASP GLY VAL GLU ASP MET SER          
SEQRES   8 X  758  GLU LEU SER TYR LEU ASN GLU PRO ALA VAL PHE HIS ASN          
SEQRES   9 X  758  LEU ARG VAL ARG TYR ASN GLN ASP LEU ILE TYR THR TYR          
SEQRES  10 X  758  SER GLY LEU PHE LEU VAL ALA VAL ASN PRO PHE LYS ARG          
SEQRES  11 X  758  ILE PRO ILE TYR THR GLN GLU MET VAL ASP ILE PHE LYS          
SEQRES  12 X  758  GLY ARG ARG ARG ASN GLU VAL ALA PRO HIS ILE PHE ALA          
SEQRES  13 X  758  ILE SER ASP VAL ALA TYR ARG SER MET LEU ASP ASP ARG          
SEQRES  14 X  758  GLN ASN GLN SER LEU LEU ILE THR GLY GLU SER GLY ALA          
SEQRES  15 X  758  GLY LYS THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU          
SEQRES  16 X  758  ALA SER VAL ALA GLY ARG ASN GLN ALA ASN GLY SER GLY          
SEQRES  17 X  758  VAL LEU GLU GLN GLN ILE LEU GLN ALA ASN PRO ILE LEU          
SEQRES  18 X  758  GLU ALA PHE GLY ASN ALA LYS THR THR ARG ASN ASN ASN          
SEQRES  19 X  758  SER SER ARG PHE GLY LYS PHE ILE GLU ILE GLN PHE ASN          
SEQRES  20 X  758  SER ALA GLY PHE ILE SER GLY ALA SER ILE GLN SER TYR          
SEQRES  21 X  758  LEU LEU GLU LYS SER ARG VAL VAL PHE GLN SER GLU THR          
SEQRES  22 X  758  GLU ARG ASN TYR HIS ILE PHE TYR GLN LEU LEU ALA GLY          
SEQRES  23 X  758  ALA THR ALA GLU GLU LYS LYS ALA LEU HIS LEU ALA GLY          
SEQRES  24 X  758  PRO GLU SER PHE ASN TYR LEU ASN GLN SER GLY CYS VAL          
SEQRES  25 X  758  ASP ILE LYS GLY VAL SER ASP SER GLU GLU PHE LYS ILE          
SEQRES  26 X  758  THR ARG GLN ALA MET ASP ILE VAL GLY PHE SER GLN GLU          
SEQRES  27 X  758  GLU GLN MET SER ILE PHE LYS ILE ILE ALA GLY ILE LEU          
SEQRES  28 X  758  HIS LEU GLY ASN ILE LYS PHE GLU LYS GLY ALA GLY GLU          
SEQRES  29 X  758  GLY ALA VAL LEU LYS ASP LYS THR ALA LEU ASN ALA ALA          
SEQRES  30 X  758  SER THR VAL PHE GLY VAL ASN PRO SER VAL LEU GLU LYS          
SEQRES  31 X  758  ALA LEU MET GLU PRO ARG ILE LEU ALA GLY ARG ASP LEU          
SEQRES  32 X  758  VAL ALA GLN HIS LEU ASN VAL GLU LYS SER SER SER SER          
SEQRES  33 X  758  ARG ASP ALA LEU VAL LYS ALA LEU TYR GLY ARG LEU PHE          
SEQRES  34 X  758  LEU TRP LEU VAL LYS LYS ILE ASN ASN VAL LEU CYS GLN          
SEQRES  35 X  758  GLU ARG LYS ALA TYR PHE ILE GLY VAL LEU ASP ILE SER          
SEQRES  36 X  758  GLY PHE GLU ILE PHE LYS VAL ASN SER PHE GLU GLN LEU          
SEQRES  37 X  758  CYS ILE ASN TYR THR ASN GLU LYS LEU GLN GLN PHE PHE          
SEQRES  38 X  758  ASN HIS HIS MET PHE LYS LEU GLU GLN GLU GLU TYR LEU          
SEQRES  39 X  758  LYS GLU LYS ILE ASN TRP THR PHE ILE ASP PHE GLY LEU          
SEQRES  40 X  758  ASP SER GLN ALA THR ILE ASP LEU ILE ASP GLY ARG GLN          
SEQRES  41 X  758  PRO PRO GLY ILE LEU ALA LEU LEU ASP GLU GLN SER VAL          
SEQRES  42 X  758  PHE PRO ASN ALA THR ASP ASN THR LEU ILE THR LYS LEU          
SEQRES  43 X  758  HIS SER HIS PHE SER LYS LYS ASN ALA LYS TYR GLU GLU          
SEQRES  44 X  758  PRO ARG PHE SER LYS THR GLU PHE GLY VAL THR HIS TYR          
SEQRES  45 X  758  ALA GLY GLN VAL MET TYR GLU ILE GLN ASP TRP LEU GLU          
SEQRES  46 X  758  LYS ASN LYS ASP PRO LEU GLN GLN ASP LEU GLU LEU CYS          
SEQRES  47 X  758  PHE LYS ASP SER SER ASP ASN VAL VAL THR LYS LEU PHE          
SEQRES  48 X  758  ASN ASP PRO ASN ILE ALA SER ARG ALA LYS LYS GLY ALA          
SEQRES  49 X  758  ASN PHE ILE THR VAL ALA ALA GLN TYR LYS GLU GLN LEU          
SEQRES  50 X  758  ALA SER LEU MET ALA THR LEU GLU THR THR ASN PRO HIS          
SEQRES  51 X  758  PHE VAL ARG CYS ILE ILE PRO ASN ASN LYS GLN LEU PRO          
SEQRES  52 X  758  ALA LYS LEU GLU ASP LYS VAL VAL LEU ASP GLN LEU ARG          
SEQRES  53 X  758  CYS ASN ALA VAL LEU GLU GLY ILE ARG ILE THR ARG LYS          
SEQRES  54 X  758  GLY PHE PRO ASN ARG ILE ILE TYR ALA ASP PHE VAL LYS          
SEQRES  55 X  758  ARG TYR TYR LEU LEU ALA PRO ASN VAL PRO ARG ASP ALA          
SEQRES  56 X  758  GLU ASP SER GLN LYS ALA THR ASP ALA VAL LEU LYS HIS          
SEQRES  57 X  758  LEU ASN ILE ASP PRO GLU GLN TYR ARG PHE GLY ILE THR          
SEQRES  58 X  758  LYS ILE PHE PHE ARG ALA GLY GLN LEU ALA ARG ILE GLU          
SEQRES  59 X  758  GLU ALA ARG GLU                                              
HET    ADP  X1001      27                                                       
HET     MG  X1002       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *258(H2 O)                                                    
HELIX    1   1 ASP X   10  LYS X   16  1                                   7    
HELIX    2   2 ASP X   90  LEU X   94  5                                   5    
HELIX    3   3 ASN X   98  GLN X  112  1                                  15    
HELIX    4   4 THR X  136  LYS X  144  1                                   9    
HELIX    5   5 HIS X  154  ARG X  170  1                                  17    
HELIX    6   6 LYS X  185  LEU X  196  1                                  12    
HELIX    7   7 VAL X  210  GLN X  217  1                                   8    
HELIX    8   8 ALA X  218  PHE X  225  1                                   8    
HELIX    9   9 SER X  266  PHE X  270  5                                   5    
HELIX   10  10 TYR X  278  GLN X  283  5                                   6    
HELIX   11  11 SER X  319  VAL X  334  1                                  16    
HELIX   12  12 SER X  337  ILE X  357  1                                  21    
HELIX   13  13 ALA X  374  GLY X  383  1                                  10    
HELIX   14  14 ASN X  385  GLU X  395  1                                  11    
HELIX   15  15 GLU X  412  CYS X  442  1                                  31    
HELIX   16  16 SER X  465  GLU X  490  1                                  26    
HELIX   17  17 SER X  510  GLY X  519  1                                  10    
HELIX   18  18 GLY X  524  SER X  533  1                                  10    
HELIX   19  19 THR X  539  HIS X  550  1                                  12    
HELIX   20  20 ASP X  583  LYS X  589  1                                   7    
HELIX   21  21 ASP X  595  LYS X  601  1                                   7    
HELIX   22  22 VAL X  608  ASP X  614  1                                   7    
HELIX   23  23 THR X  629  ALA X  643  1                                  15    
HELIX   24  24 VAL X  671  ARG X  677  1                                   7    
HELIX   25  25 ASN X  679  GLY X  684  1                                   6    
HELIX   26  26 ILE X  685  LYS X  690  1                                   6    
HELIX   27  27 ASP X  700  TYR X  705  1                                   6    
HELIX   28  28 ASP X  718  THR X  723  1                                   6    
HELIX   29  29 ASP X  724  LEU X  727  5                                   4    
HELIX   30  30 ASP X  733  TYR X  737  5                                   5    
HELIX   31  31 LEU X  751  GLU X  756  1                                   6    
SHEET    1  XA 3 GLU X  48  GLU X  51  0                                        
SHEET    2  XA 3 TYR X  34  TYR X  37 -1  O  ILE X  35   N  GLY X  50           
SHEET    3  XA 3 ASN X  78  GLN X  79 -1  O  ASN X  78   N  TRP X  36           
SHEET    1  XB 7 TYR X 116  TYR X 118  0                                        
SHEET    2  XB 7 LEU X 123  VAL X 126 -1  O  VAL X 124   N  THR X 117           
SHEET    3  XB 7 ASN X 649  ILE X 656  1  O  PHE X 652   N  LEU X 123           
SHEET    4  XB 7 GLN X 173  GLY X 179  1  O  SER X 174   N  HIS X 651           
SHEET    5  XB 7 ALA X 447  ASP X 454  1  O  PHE X 449   N  GLN X 173           
SHEET    6  XB 7 ILE X 245  PHE X 247 -1  O  ILE X 245   N  ILE X 450           
SHEET    7  XB 7 ILE X 253  ALA X 256 -1  N  SER X 254   O  GLN X 246           
SHEET    1  XC 6 TYR X 116  TYR X 118  0                                        
SHEET    2  XC 6 LEU X 123  VAL X 126 -1  O  VAL X 124   N  THR X 117           
SHEET    3  XC 6 ASN X 649  ILE X 656  1  O  PHE X 652   N  LEU X 123           
SHEET    4  XC 6 GLN X 173  GLY X 179  1  O  SER X 174   N  HIS X 651           
SHEET    5  XC 6 ALA X 447  ASP X 454  1  O  PHE X 449   N  GLN X 173           
SHEET    6  XC 6 LYS X 241  ILE X 243 -1  O  LYS X 241   N  ASP X 454           
SHEET    1  XD 2 ASN X 227  THR X 230  0                                        
SHEET    2  XD 2 ASN X 233  SER X 237 -1  O  ASN X 233   N  THR X 230           
SHEET    1  XE 2 GLU X 360  LYS X 361  0                                        
SHEET    2  XE 2 ALA X 367  VAL X 368 -1  O  VAL X 368   N  GLU X 360           
SHEET    1  XF 2 ARG X 397  ALA X 400  0                                        
SHEET    2  XF 2 ASP X 403  ALA X 406 -1  O  ASP X 403   N  ALA X 400           
SHEET    1  XG 2 PHE X 568  HIS X 572  0                                        
SHEET    2  XG 2 GLY X 575  TYR X 579 -1  O  GLY X 575   N  HIS X 572           
LINK         OG1 THR X 186                MG    MG X1002     1555   1555  1.83  
LINK         OG  SER X 237                MG    MG X1002     1555   1555  2.72  
LINK         OD2 ASP X 454                MG    MG X1002     1555   1555  2.78  
CISPEP   1 GLN X  521    PRO X  522          0         0.07                     
SITE     1 AC1 15 ASN X 127  PRO X 128  LYS X 130  TYR X 135                    
SITE     2 AC1 15 GLY X 182  GLY X 184  LYS X 185  THR X 186                    
SITE     3 AC1 15 GLU X 187  ASN X 233   MG X1002  HOH X2068                    
SITE     4 AC1 15 HOH X2256  HOH X2257  HOH X2258                               
SITE     1 AC2  4 THR X 186  SER X 237  ASP X 454  ADP X1001                    
CRYST1   55.000  105.800  180.500  90.00  90.00  90.00 P 2 21 21     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      0.018182  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009452  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system