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Database: PDB
Entry: 4BYF
LinkDB: 4BYF
Original site: 4BYF 
HEADER    HYDROLASE                               19-JUL-13   4BYF              
TITLE     CRYSTAL STRUCTURE OF HUMAN MYOSIN 1C IN COMPLEX WITH CALMODULIN IN THE
TITLE    2 PRE-POWER STROKE STATE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCONVENTIONAL MYOSIN-IC;                                  
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: MOTOR DOMAIN, RESIDUES 36-760;                             
COMPND   5 SYNONYM: MYOSIN I BETA, MMI-BETA, MMIB;                              
COMPND   6 EC: 3.6.4.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CALMODULIN;                                                
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 SYNONYM: CAM;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;                            
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL                             
KEYWDS    HYDROLASE, MYO1C, GLUT4 EXOCYTOSIS, ATPASE, MOTOR PROTEIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MUNNICH,M.H.TAFT,S.PATHAN-CHHATBAR,D.J.MANSTEIN                     
REVDAT   3   20-DEC-23 4BYF    1       REMARK LINK                              
REVDAT   2   14-MAY-14 4BYF    1       JRNL                                     
REVDAT   1   26-MAR-14 4BYF    0                                                
JRNL        AUTH   S.MUNNICH,M.H.TAFT,D.J.MANSTEIN                              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN MYOSIN 1C-THE MOTOR IN GLUT4      
JRNL        TITL 2 EXOCYTOSIS: IMPLICATIONS FOR CA(2+) REGULATION AND 14-3-3    
JRNL        TITL 3 BINDING.                                                     
JRNL        REF    J.MOL.BIOL.                   V. 426  2070 2014              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   24636949                                                     
JRNL        DOI    10.1016/J.JMB.2014.03.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 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) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 51985                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 2.00                                          
REMARK   3   SHRINKAGE RADIUS   : 2.00                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.834           NULL                                  
REMARK   3   ANGLE     :  0.005           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 4BYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290057287.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.06450                            
REMARK 200  MONOCHROMATOR                  : SILICON (1 1 1) CHANNEL-CUT        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51985                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.85000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.150                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1LKX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2 M SODIUM MALONATE PH    
REMARK 280  7.0                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       79.22500            
REMARK 290   SMTRY3   2  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: 3820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.7 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 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: 3640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     ILE A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     GLN A   496                                                      
REMARK 465     ARG A   497                                                      
REMARK 465     THR A   498                                                      
REMARK 465     LEU A   556                                                      
REMARK 465     SER A   557                                                      
REMARK 465     ASP A   558                                                      
REMARK 465     LYS A   559                                                      
REMARK 465     ARG A   721                                                      
REMARK 465     VAL A   722                                                      
REMARK 465     LYS A   723                                                      
REMARK 465     ARG A   724                                                      
REMARK 465     SER A   725                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     GLU C   289                                                      
REMARK 465     SER C   290                                                      
REMARK 465     ILE C   324                                                      
REMARK 465     ALA C   325                                                      
REMARK 465     LYS C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLU C   328                                                      
REMARK 465     GLN C   496                                                      
REMARK 465     ARG C   497                                                      
REMARK 465     THR C   498                                                      
REMARK 465     GLU C   555                                                      
REMARK 465     LEU C   556                                                      
REMARK 465     SER C   557                                                      
REMARK 465     ASP C   558                                                      
REMARK 465     LYS C   559                                                      
REMARK 465     ARG C   721                                                      
REMARK 465     VAL C   722                                                      
REMARK 465     LYS C   723                                                      
REMARK 465     ARG C   724                                                      
REMARK 465     SER C   725                                                      
REMARK 465     MET D     1                                                      
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  MG     MG A  1000    H2G1  AOV A  1001              1.36            
REMARK 500  MG     MG C  1000     O2G  AOV C  1001              1.59            
REMARK 500   O    LYS C   451     N    LYS C   453              1.97            
REMARK 500   O    PHE A   627     NH2  ARG A   630              2.08            
REMARK 500   OG   SER A   375     OG   SER A   378              2.09            
REMARK 500   O    PHE C   627     NH2  ARG C   630              2.13            
REMARK 500   O    HOH C  2050     O    HOH C  2051              2.15            
REMARK 500   OE2  GLU A   422     NH2  ARG A   623              2.16            
REMARK 500   NH2  ARG A   465     OE2  GLU A   468              2.17            
REMARK 500   OG   SER C   107     O1G  AOV C  1001              2.18            
REMARK 500   NZ   LYS C   111     O2B  AOV C  1001              2.19            
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    PRO C  79   C   -  N   -  CD  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO C 562   C   -  N   -  CA  ANGL. DEV. =  10.3 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    ARG A  96       74.38     45.66                                   
REMARK 500    THR A 125      -62.91    -95.56                                   
REMARK 500    GLU A 130      -74.28    -89.51                                   
REMARK 500    ALA A 134       -2.17     94.30                                   
REMARK 500    LEU A 186       74.51     41.57                                   
REMARK 500    GLN A 236       -2.12     70.77                                   
REMARK 500    ASP A 260       39.84     70.73                                   
REMARK 500    ALA A 285      -78.99   -108.97                                   
REMARK 500    ALA A 286      163.96    172.55                                   
REMARK 500    ASN A 287      -67.78   -129.24                                   
REMARK 500    GLU A 372       -7.39     64.77                                   
REMARK 500    SER A 375     -159.57    -81.44                                   
REMARK 500    TRP A 376       -6.20     94.53                                   
REMARK 500    SER A 397     -168.87   -127.06                                   
REMARK 500    LEU A 419      -63.56   -129.54                                   
REMARK 500    VAL A 448      -63.89    -90.43                                   
REMARK 500    PHE A 452      -20.67     75.26                                   
REMARK 500    ARG A 465      147.20     76.95                                   
REMARK 500    GLU A 468      -64.70   -129.70                                   
REMARK 500    HIS A 484       72.68     43.31                                   
REMARK 500    ALA A 494     -139.97     56.11                                   
REMARK 500    ARG A 499      142.36   -172.07                                   
REMARK 500    ARG A 561       75.35     51.75                                   
REMARK 500    ARG A 677      -71.16    -57.59                                   
REMARK 500    LYS B  22     -114.45     55.75                                   
REMARK 500    ASN B  43       69.27   -117.94                                   
REMARK 500    ASN B  61      -13.45     74.36                                   
REMARK 500    THR C 125      -62.02    -95.38                                   
REMARK 500    GLU C 130      -74.37    -94.49                                   
REMARK 500    LEU C 186       75.32     42.37                                   
REMARK 500    VAL C 233       69.60   -115.73                                   
REMARK 500    GLN C 236       -2.76     68.83                                   
REMARK 500    ALA C 285      -79.72   -107.65                                   
REMARK 500    ALA C 286      160.41    172.37                                   
REMARK 500    ASN C 287      -66.83   -132.59                                   
REMARK 500    VAL C 371      -79.49    -92.48                                   
REMARK 500    SER C 373      167.93     66.56                                   
REMARK 500    SER C 375      -60.81    -98.78                                   
REMARK 500    TRP C 376       -8.20     89.04                                   
REMARK 500    SER C 397     -168.75   -126.61                                   
REMARK 500    LEU C 419      -64.64   -129.10                                   
REMARK 500    VAL C 448      -64.34    -91.26                                   
REMARK 500    PHE C 452      -46.56     58.93                                   
REMARK 500    ARG C 465      150.09     74.90                                   
REMARK 500    GLU C 468      -65.14   -127.36                                   
REMARK 500    HIS C 484       72.33     43.18                                   
REMARK 500    ALA C 494     -138.78     57.64                                   
REMARK 500    ARG C 499      139.00   -172.22                                   
REMARK 500    ARG C 553     -120.88     46.87                                   
REMARK 500    ARG C 677      -70.39    -55.79                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2001        DISTANCE =  7.01 ANGSTROMS                       
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 A1000  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 112   OG1                                                    
REMARK 620 2 SER A 161   OG   89.2                                              
REMARK 620 3 AOV A1001   O1B 103.0 166.3                                        
REMARK 620 4 AOV A1001   O2G 171.5  83.3  84.9                                  
REMARK 620 5 HOH A2010   O   103.2  91.2  80.0  81.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1000  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 112   OG1                                                    
REMARK 620 2 SER C 161   OG   84.9                                              
REMARK 620 3 AOV C1001   O1B  83.8 158.6                                        
REMARK 620 4 HOH C2019   O    73.0  75.5  83.8                                  
REMARK 620 5 HOH C2021   O    83.8  96.7 100.1 156.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1000  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  94   OD1                                                    
REMARK 620 2 ASP D  96   OD2 133.1                                              
REMARK 620 3 ASN D  98   OD1  92.7  75.7                                        
REMARK 620 4 TYR D 100   O    92.9 131.7  90.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOV A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOV C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1000                 
DBREF  4BYF A    1   725  UNP    O00159   MYO1C_HUMAN     36    760             
DBREF  4BYF B    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4BYF C    1   725  UNP    O00159   MYO1C_HUMAN     36    760             
DBREF  4BYF D    1   149  UNP    P62158   CALM_HUMAN       1    149             
SEQRES   1 A  725  MET GLU SER ALA LEU THR ALA ARG ASP ARG VAL GLY VAL          
SEQRES   2 A  725  GLN ASP PHE VAL LEU LEU GLU ASN PHE THR SER GLU ALA          
SEQRES   3 A  725  ALA PHE ILE GLU ASN LEU ARG ARG ARG PHE ARG GLU ASN          
SEQRES   4 A  725  LEU ILE TYR THR TYR ILE GLY PRO VAL LEU VAL SER VAL          
SEQRES   5 A  725  ASN PRO TYR ARG ASP LEU GLN ILE TYR SER ARG GLN HIS          
SEQRES   6 A  725  MET GLU ARG TYR ARG GLY VAL SER PHE TYR GLU VAL PRO          
SEQRES   7 A  725  PRO HIS LEU PHE ALA VAL ALA ASP THR VAL TYR ARG ALA          
SEQRES   8 A  725  LEU ARG THR GLU ARG ARG ASP GLN ALA VAL MET ILE SER          
SEQRES   9 A  725  GLY GLU SER GLY ALA GLY LYS THR GLU ALA THR LYS ARG          
SEQRES  10 A  725  LEU LEU GLN PHE TYR ALA GLU THR CYS PRO ALA PRO GLU          
SEQRES  11 A  725  ARG GLY GLY ALA VAL ARG ASP ARG LEU LEU GLN SER ASN          
SEQRES  12 A  725  PRO VAL LEU GLU ALA PHE GLY ASN ALA LYS THR LEU ARG          
SEQRES  13 A  725  ASN ASP ASN SER SER ARG PHE GLY LYS TYR MET ASP VAL          
SEQRES  14 A  725  GLN PHE ASP PHE LYS GLY ALA PRO VAL GLY GLY HIS ILE          
SEQRES  15 A  725  LEU SER TYR LEU LEU GLU LYS SER ARG VAL VAL HIS GLN          
SEQRES  16 A  725  ASN HIS GLY GLU ARG ASN PHE HIS ILE PHE TYR GLN LEU          
SEQRES  17 A  725  LEU GLU GLY GLY GLU GLU GLU THR LEU ARG ARG LEU GLY          
SEQRES  18 A  725  LEU GLU ARG ASN PRO GLN SER TYR LEU TYR LEU VAL LYS          
SEQRES  19 A  725  GLY GLN CYS ALA LYS VAL SER SER ILE ASN ASP LYS SER          
SEQRES  20 A  725  ASP TRP LYS VAL VAL ARG LYS ALA LEU THR VAL ILE ASP          
SEQRES  21 A  725  PHE THR GLU ASP GLU VAL GLU ASP LEU LEU SER ILE VAL          
SEQRES  22 A  725  ALA SER VAL LEU HIS LEU GLY ASN ILE HIS PHE ALA ALA          
SEQRES  23 A  725  ASN GLU GLU SER ASN ALA GLN VAL THR THR GLU ASN GLN          
SEQRES  24 A  725  LEU LYS TYR LEU THR ARG LEU LEU SER VAL GLU GLY SER          
SEQRES  25 A  725  THR LEU ARG GLU ALA LEU THR HIS ARG LYS ILE ILE ALA          
SEQRES  26 A  725  LYS GLY GLU GLU LEU LEU SER PRO LEU ASN LEU GLU GLN          
SEQRES  27 A  725  ALA ALA TYR ALA ARG ASP ALA LEU ALA LYS ALA VAL TYR          
SEQRES  28 A  725  SER ARG THR PHE THR TRP LEU VAL GLY LYS ILE ASN ARG          
SEQRES  29 A  725  SER LEU ALA SER LYS ASP VAL GLU SER PRO SER TRP ARG          
SEQRES  30 A  725  SER THR THR VAL LEU GLY LEU LEU ASP ILE TYR GLY PHE          
SEQRES  31 A  725  GLU VAL PHE GLN HIS ASN SER PHE GLU GLN PHE CYS ILE          
SEQRES  32 A  725  ASN TYR CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU          
SEQRES  33 A  725  LEU THR LEU LYS SER GLU GLN GLU GLU TYR GLU ALA GLU          
SEQRES  34 A  725  GLY ILE ALA TRP GLU PRO VAL GLN TYR PHE ASN ASN LYS          
SEQRES  35 A  725  ILE ILE CYS ASP LEU VAL GLU GLU LYS PHE LYS GLY ILE          
SEQRES  36 A  725  ILE SER ILE LEU ASP GLU GLU CYS LEU ARG PRO GLY GLU          
SEQRES  37 A  725  ALA THR ASP LEU THR PHE LEU GLU LYS LEU GLU ASP THR          
SEQRES  38 A  725  VAL LYS HIS HIS PRO HIS PHE LEU THR HIS LYS LEU ALA          
SEQRES  39 A  725  ASP GLN ARG THR ARG LYS SER LEU GLY ARG GLY GLU PHE          
SEQRES  40 A  725  ARG LEU LEU HIS TYR ALA GLY GLU VAL THR TYR SER VAL          
SEQRES  41 A  725  THR GLY PHE LEU ASP LYS ASN ASN ASP LEU LEU PHE ARG          
SEQRES  42 A  725  ASN LEU LYS GLU THR MET CYS SER SER LYS ASN PRO ILE          
SEQRES  43 A  725  MET SER GLN CYS PHE ASP ARG SER GLU LEU SER ASP LYS          
SEQRES  44 A  725  LYS ARG PRO GLU THR VAL ALA THR GLN PHE LYS MET SER          
SEQRES  45 A  725  LEU LEU GLN LEU VAL GLU ILE LEU GLN SER LYS GLU PRO          
SEQRES  46 A  725  ALA TYR VAL ARG CYS ILE LYS PRO ASN ASP ALA LYS GLN          
SEQRES  47 A  725  PRO GLY ARG PHE ASP GLU VAL LEU ILE ARG HIS GLN VAL          
SEQRES  48 A  725  LYS TYR LEU GLY LEU LEU GLU ASN LEU ARG VAL ARG ARG          
SEQRES  49 A  725  ALA GLY PHE ALA TYR ARG ARG LYS TYR GLU ALA PHE LEU          
SEQRES  50 A  725  GLN ARG TYR LYS SER LEU CYS PRO GLU THR TRP PRO THR          
SEQRES  51 A  725  TRP ALA GLY ARG PRO GLN ASP GLY VAL ALA VAL LEU VAL          
SEQRES  52 A  725  ARG HIS LEU GLY TYR LYS PRO GLU GLU TYR LYS MET GLY          
SEQRES  53 A  725  ARG THR LYS ILE PHE ILE ARG PHE PRO LYS THR LEU PHE          
SEQRES  54 A  725  ALA THR GLU ASP ALA LEU GLU VAL ARG ARG GLN SER LEU          
SEQRES  55 A  725  ALA THR LYS ILE GLN ALA ALA TRP ARG GLY PHE HIS TRP          
SEQRES  56 A  725  ARG GLN LYS PHE LEU ARG VAL LYS ARG SER                      
SEQRES   1 B  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 B  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 B  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 B  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 B  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 B  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 B  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 B  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 B  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 B  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 B  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 B  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 C  725  MET GLU SER ALA LEU THR ALA ARG ASP ARG VAL GLY VAL          
SEQRES   2 C  725  GLN ASP PHE VAL LEU LEU GLU ASN PHE THR SER GLU ALA          
SEQRES   3 C  725  ALA PHE ILE GLU ASN LEU ARG ARG ARG PHE ARG GLU ASN          
SEQRES   4 C  725  LEU ILE TYR THR TYR ILE GLY PRO VAL LEU VAL SER VAL          
SEQRES   5 C  725  ASN PRO TYR ARG ASP LEU GLN ILE TYR SER ARG GLN HIS          
SEQRES   6 C  725  MET GLU ARG TYR ARG GLY VAL SER PHE TYR GLU VAL PRO          
SEQRES   7 C  725  PRO HIS LEU PHE ALA VAL ALA ASP THR VAL TYR ARG ALA          
SEQRES   8 C  725  LEU ARG THR GLU ARG ARG ASP GLN ALA VAL MET ILE SER          
SEQRES   9 C  725  GLY GLU SER GLY ALA GLY LYS THR GLU ALA THR LYS ARG          
SEQRES  10 C  725  LEU LEU GLN PHE TYR ALA GLU THR CYS PRO ALA PRO GLU          
SEQRES  11 C  725  ARG GLY GLY ALA VAL ARG ASP ARG LEU LEU GLN SER ASN          
SEQRES  12 C  725  PRO VAL LEU GLU ALA PHE GLY ASN ALA LYS THR LEU ARG          
SEQRES  13 C  725  ASN ASP ASN SER SER ARG PHE GLY LYS TYR MET ASP VAL          
SEQRES  14 C  725  GLN PHE ASP PHE LYS GLY ALA PRO VAL GLY GLY HIS ILE          
SEQRES  15 C  725  LEU SER TYR LEU LEU GLU LYS SER ARG VAL VAL HIS GLN          
SEQRES  16 C  725  ASN HIS GLY GLU ARG ASN PHE HIS ILE PHE TYR GLN LEU          
SEQRES  17 C  725  LEU GLU GLY GLY GLU GLU GLU THR LEU ARG ARG LEU GLY          
SEQRES  18 C  725  LEU GLU ARG ASN PRO GLN SER TYR LEU TYR LEU VAL LYS          
SEQRES  19 C  725  GLY GLN CYS ALA LYS VAL SER SER ILE ASN ASP LYS SER          
SEQRES  20 C  725  ASP TRP LYS VAL VAL ARG LYS ALA LEU THR VAL ILE ASP          
SEQRES  21 C  725  PHE THR GLU ASP GLU VAL GLU ASP LEU LEU SER ILE VAL          
SEQRES  22 C  725  ALA SER VAL LEU HIS LEU GLY ASN ILE HIS PHE ALA ALA          
SEQRES  23 C  725  ASN GLU GLU SER ASN ALA GLN VAL THR THR GLU ASN GLN          
SEQRES  24 C  725  LEU LYS TYR LEU THR ARG LEU LEU SER VAL GLU GLY SER          
SEQRES  25 C  725  THR LEU ARG GLU ALA LEU THR HIS ARG LYS ILE ILE ALA          
SEQRES  26 C  725  LYS GLY GLU GLU LEU LEU SER PRO LEU ASN LEU GLU GLN          
SEQRES  27 C  725  ALA ALA TYR ALA ARG ASP ALA LEU ALA LYS ALA VAL TYR          
SEQRES  28 C  725  SER ARG THR PHE THR TRP LEU VAL GLY LYS ILE ASN ARG          
SEQRES  29 C  725  SER LEU ALA SER LYS ASP VAL GLU SER PRO SER TRP ARG          
SEQRES  30 C  725  SER THR THR VAL LEU GLY LEU LEU ASP ILE TYR GLY PHE          
SEQRES  31 C  725  GLU VAL PHE GLN HIS ASN SER PHE GLU GLN PHE CYS ILE          
SEQRES  32 C  725  ASN TYR CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU          
SEQRES  33 C  725  LEU THR LEU LYS SER GLU GLN GLU GLU TYR GLU ALA GLU          
SEQRES  34 C  725  GLY ILE ALA TRP GLU PRO VAL GLN TYR PHE ASN ASN LYS          
SEQRES  35 C  725  ILE ILE CYS ASP LEU VAL GLU GLU LYS PHE LYS GLY ILE          
SEQRES  36 C  725  ILE SER ILE LEU ASP GLU GLU CYS LEU ARG PRO GLY GLU          
SEQRES  37 C  725  ALA THR ASP LEU THR PHE LEU GLU LYS LEU GLU ASP THR          
SEQRES  38 C  725  VAL LYS HIS HIS PRO HIS PHE LEU THR HIS LYS LEU ALA          
SEQRES  39 C  725  ASP GLN ARG THR ARG LYS SER LEU GLY ARG GLY GLU PHE          
SEQRES  40 C  725  ARG LEU LEU HIS TYR ALA GLY GLU VAL THR TYR SER VAL          
SEQRES  41 C  725  THR GLY PHE LEU ASP LYS ASN ASN ASP LEU LEU PHE ARG          
SEQRES  42 C  725  ASN LEU LYS GLU THR MET CYS SER SER LYS ASN PRO ILE          
SEQRES  43 C  725  MET SER GLN CYS PHE ASP ARG SER GLU LEU SER ASP LYS          
SEQRES  44 C  725  LYS ARG PRO GLU THR VAL ALA THR GLN PHE LYS MET SER          
SEQRES  45 C  725  LEU LEU GLN LEU VAL GLU ILE LEU GLN SER LYS GLU PRO          
SEQRES  46 C  725  ALA TYR VAL ARG CYS ILE LYS PRO ASN ASP ALA LYS GLN          
SEQRES  47 C  725  PRO GLY ARG PHE ASP GLU VAL LEU ILE ARG HIS GLN VAL          
SEQRES  48 C  725  LYS TYR LEU GLY LEU LEU GLU ASN LEU ARG VAL ARG ARG          
SEQRES  49 C  725  ALA GLY PHE ALA TYR ARG ARG LYS TYR GLU ALA PHE LEU          
SEQRES  50 C  725  GLN ARG TYR LYS SER LEU CYS PRO GLU THR TRP PRO THR          
SEQRES  51 C  725  TRP ALA GLY ARG PRO GLN ASP GLY VAL ALA VAL LEU VAL          
SEQRES  52 C  725  ARG HIS LEU GLY TYR LYS PRO GLU GLU TYR LYS MET GLY          
SEQRES  53 C  725  ARG THR LYS ILE PHE ILE ARG PHE PRO LYS THR LEU PHE          
SEQRES  54 C  725  ALA THR GLU ASP ALA LEU GLU VAL ARG ARG GLN SER LEU          
SEQRES  55 C  725  ALA THR LYS ILE GLN ALA ALA TRP ARG GLY PHE HIS TRP          
SEQRES  56 C  725  ARG GLN LYS PHE LEU ARG VAL LYS ARG SER                      
SEQRES   1 D  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 D  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 D  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 D  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 D  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 D  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 D  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 D  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 D  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 D  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 D  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 D  149  GLN MET MET THR ALA LYS                                      
HET     MG  A1000       1                                                       
HET    AOV  A1001      47                                                       
HET     MG  C1000       1                                                       
HET    AOV  C1001      47                                                       
HET     MG  D1000       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     AOV ADP ORTHOVANADATE                                                
FORMUL   5   MG    3(MG 2+)                                                     
FORMUL   6  AOV    2(C10 H17 N5 O14 P2 V)                                       
FORMUL  10  HOH   *194(H2 O)                                                    
HELIX    1   1 PHE A   16  LEU A   19  5                                   4    
HELIX    2   2 SER A   24  GLU A   38  1                                  15    
HELIX    3   3 SER A   62  ARG A   70  1                                   9    
HELIX    4   4 SER A   73  VAL A   77  5                                   5    
HELIX    5   5 HIS A   80  GLU A   95  1                                  16    
HELIX    6   6 GLY A  110  CYS A  126  1                                  17    
HELIX    7   7 ALA A  134  GLY A  150  1                                  17    
HELIX    8   8 LYS A  189  VAL A  193  5                                   5    
HELIX    9   9 PHE A  202  GLY A  212  1                                  11    
HELIX   10  10 GLU A  213  LEU A  220  1                                   8    
HELIX   11  11 ASN A  225  TYR A  229  5                                   5    
HELIX   12  12 ASN A  244  ILE A  259  1                                  16    
HELIX   13  13 THR A  262  ILE A  282  1                                  21    
HELIX   14  14 GLU A  297  SER A  308  1                                  12    
HELIX   15  15 GLU A  310  THR A  319  1                                  10    
HELIX   16  16 ASN A  335  ALA A  367  1                                  33    
HELIX   17  17 SER A  397  LEU A  419  1                                  23    
HELIX   18  18 LEU A  419  GLY A  430  1                                  12    
HELIX   19  19 ASN A  441  GLU A  450  1                                  10    
HELIX   20  20 GLY A  454  GLU A  462  1                                   9    
HELIX   21  21 THR A  470  VAL A  482  1                                  13    
HELIX   22  22 GLY A  522  ASN A  528  1                                   7    
HELIX   23  23 PHE A  532  SER A  541  1                                  10    
HELIX   24  24 ASN A  544  PHE A  551  1                                   8    
HELIX   25  25 THR A  564  SER A  582  1                                  19    
HELIX   26  26 ASP A  603  GLY A  615  1                                  13    
HELIX   27  27 GLY A  615  GLY A  626  1                                  12    
HELIX   28  28 TYR A  633  LYS A  641  1                                   9    
HELIX   29  29 SER A  642  CYS A  644  5                                   3    
HELIX   30  30 ARG A  654  GLY A  667  1                                  14    
HELIX   31  31 PHE A  684  PHE A  719  1                                  36    
HELIX   32  32 THR B    6  PHE B   20  1                                  15    
HELIX   33  33 GLU B   32  LEU B   40  1                                   9    
HELIX   34  34 THR B   45  ASP B   57  1                                  13    
HELIX   35  35 PHE B   66  MET B   77  1                                  12    
HELIX   36  36 SER B   82  ASP B   94  1                                  13    
HELIX   37  37 ALA B  103  LEU B  113  1                                  11    
HELIX   38  38 THR B  118  ASP B  130  1                                  13    
HELIX   39  39 TYR B  139  ALA B  148  1                                  10    
HELIX   40  40 PHE C   16  LEU C   19  5                                   4    
HELIX   41  41 SER C   24  GLU C   38  1                                  15    
HELIX   42  42 SER C   62  ARG C   70  1                                   9    
HELIX   43  43 SER C   73  VAL C   77  5                                   5    
HELIX   44  44 HIS C   80  GLU C   95  1                                  16    
HELIX   45  45 GLY C  110  CYS C  126  1                                  17    
HELIX   46  46 VAL C  135  GLY C  150  1                                  16    
HELIX   47  47 LYS C  189  VAL C  193  5                                   5    
HELIX   48  48 PHE C  202  GLY C  212  1                                  11    
HELIX   49  49 GLU C  213  LEU C  220  1                                   8    
HELIX   50  50 ASN C  225  TYR C  229  5                                   5    
HELIX   51  51 ASN C  244  ILE C  259  1                                  16    
HELIX   52  52 THR C  262  ILE C  282  1                                  21    
HELIX   53  53 GLU C  297  SER C  308  1                                  12    
HELIX   54  54 GLU C  310  THR C  319  1                                  10    
HELIX   55  55 ASN C  335  ALA C  367  1                                  33    
HELIX   56  56 SER C  397  LEU C  419  1                                  23    
HELIX   57  57 LEU C  419  GLU C  429  1                                  11    
HELIX   58  58 ASN C  441  GLU C  450  1                                  10    
HELIX   59  59 GLY C  454  GLU C  462  1                                   9    
HELIX   60  60 THR C  470  VAL C  482  1                                  13    
HELIX   61  61 GLY C  522  ASN C  528  1                                   7    
HELIX   62  62 PHE C  532  SER C  541  1                                  10    
HELIX   63  63 ASN C  544  PHE C  551  1                                   8    
HELIX   64  64 THR C  564  SER C  582  1                                  19    
HELIX   65  65 ASP C  603  GLY C  615  1                                  13    
HELIX   66  66 GLY C  615  GLY C  626  1                                  12    
HELIX   67  67 TYR C  633  LYS C  641  1                                   9    
HELIX   68  68 SER C  642  CYS C  644  5                                   3    
HELIX   69  69 ARG C  654  GLY C  667  1                                  14    
HELIX   70  70 PHE C  684  PHE C  719  1                                  36    
HELIX   71  71 THR D    6  PHE D   20  1                                  15    
HELIX   72  72 GLU D   32  LEU D   40  1                                   9    
HELIX   73  73 THR D   45  ASP D   57  1                                  13    
HELIX   74  74 PHE D   66  ASP D   79  1                                  14    
HELIX   75  75 SER D   82  ASP D   94  1                                  13    
HELIX   76  76 ALA D  103  LEU D  113  1                                  11    
HELIX   77  77 THR D  118  ASP D  130  1                                  13    
HELIX   78  78 TYR D  139  ALA D  148  1                                  10    
SHEET    1  AA 7 TYR A  42  ILE A  45  0                                        
SHEET    2  AA 7 VAL A  48  VAL A  52 -1  O  VAL A  48   N  ILE A  45           
SHEET    3  AA 7 GLU A 584  ILE A 591  1  O  TYR A 587   N  LEU A  49           
SHEET    4  AA 7 GLN A  99  SER A 104  1  O  ALA A 100   N  ALA A 586           
SHEET    5  AA 7 THR A 380  ASP A 386  1  O  VAL A 381   N  GLN A  99           
SHEET    6  AA 7 GLY A 164  PHE A 171 -1  O  LYS A 165   N  ASP A 386           
SHEET    7  AA 7 PRO A 177  TYR A 185 -1  N  VAL A 178   O  GLN A 170           
SHEET    1  AB 2 ASN A 151  ALA A 152  0                                        
SHEET    2  AB 2 SER A 160  SER A 161 -1  O  SER A 160   N  ALA A 152           
SHEET    1  AC 2 HIS A 320  LYS A 322  0                                        
SHEET    2  AC 2 LEU A 331  PRO A 333 -1  O  SER A 332   N  ARG A 321           
SHEET    1  AD 3 PHE A 488  LEU A 489  0                                        
SHEET    2  AD 3 GLU A 506  HIS A 511 -1  O  ARG A 508   N  LEU A 489           
SHEET    3  AD 3 GLY A 514  SER A 519 -1  O  GLY A 514   N  HIS A 511           
SHEET    1  AE 3 TYR A 629  LYS A 632  0                                        
SHEET    2  AE 3 LYS A 679  ILE A 682 -1  O  ILE A 680   N  ARG A 631           
SHEET    3  AE 3 TYR A 673  MET A 675 -1  O  LYS A 674   N  PHE A 681           
SHEET    1  BA 2 THR B  27  THR B  29  0                                        
SHEET    2  BA 2 THR B  63  ASP B  65 -1  O  ILE B  64   N  ILE B  28           
SHEET    1  BB 2 TYR B 100  SER B 102  0                                        
SHEET    2  BB 2 GLN B 136  ASN B 138 -1  O  VAL B 137   N  ILE B 101           
SHEET    1  CA 7 TYR C  42  ILE C  45  0                                        
SHEET    2  CA 7 VAL C  48  VAL C  52 -1  O  VAL C  48   N  ILE C  45           
SHEET    3  CA 7 GLU C 584  ILE C 591  1  O  TYR C 587   N  LEU C  49           
SHEET    4  CA 7 GLN C  99  SER C 104  1  O  ALA C 100   N  ALA C 586           
SHEET    5  CA 7 THR C 380  ASP C 386  1  O  VAL C 381   N  GLN C  99           
SHEET    6  CA 7 GLY C 164  PHE C 171 -1  O  LYS C 165   N  ASP C 386           
SHEET    7  CA 7 PRO C 177  TYR C 185 -1  N  VAL C 178   O  GLN C 170           
SHEET    1  CB 2 ASN C 151  ALA C 152  0                                        
SHEET    2  CB 2 SER C 160  SER C 161 -1  O  SER C 160   N  ALA C 152           
SHEET    1  CC 2 HIS C 320  LYS C 322  0                                        
SHEET    2  CC 2 LEU C 331  PRO C 333 -1  O  SER C 332   N  ARG C 321           
SHEET    1  CD 3 PHE C 488  THR C 490  0                                        
SHEET    2  CD 3 GLU C 506  HIS C 511 -1  O  ARG C 508   N  LEU C 489           
SHEET    3  CD 3 GLY C 514  SER C 519 -1  O  GLY C 514   N  HIS C 511           
SHEET    1  CE 3 TYR C 629  LYS C 632  0                                        
SHEET    2  CE 3 LYS C 679  ILE C 682 -1  O  ILE C 680   N  ARG C 631           
SHEET    3  CE 3 TYR C 673  MET C 675 -1  O  LYS C 674   N  PHE C 681           
SHEET    1  DA 2 THR D  27  THR D  29  0                                        
SHEET    2  DA 2 THR D  63  ASP D  65 -1  O  ILE D  64   N  ILE D  28           
SHEET    1  DB 2 TYR D 100  SER D 102  0                                        
SHEET    2  DB 2 GLN D 136  ASN D 138 -1  O  VAL D 137   N  ILE D 101           
LINK         OG1 THR A 112                MG    MG A1000     1555   1555  1.67  
LINK         OG  SER A 161                MG    MG A1000     1555   1555  2.46  
LINK        MG    MG A1000                 O1B AOV A1001     1555   1555  2.16  
LINK        MG    MG A1000                 O2G AOV A1001     1555   1555  1.99  
LINK        MG    MG A1000                 O   HOH A2010     1555   1555  2.14  
LINK         OG1 THR C 112                MG    MG C1000     1555   1555  2.10  
LINK         OG  SER C 161                MG    MG C1000     1555   1555  2.60  
LINK        MG    MG C1000                 O1B AOV C1001     1555   1555  2.24  
LINK        MG    MG C1000                 O   HOH C2019     1555   1555  1.91  
LINK        MG    MG C1000                 O   HOH C2021     1555   1555  1.73  
LINK         OD1 ASP D  94                MG    MG D1000     1555   1555  2.15  
LINK         OD2 ASP D  96                MG    MG D1000     1555   1555  2.85  
LINK         OD1 ASN D  98                MG    MG D1000     1555   1555  2.44  
LINK         O   TYR D 100                MG    MG D1000     1555   1555  2.38  
CISPEP   1 PRO A  374    SER A  375          0         7.50                     
CISPEP   2 ARG A  499    LYS A  500          0        14.89                     
CISPEP   3 LYS A  500    SER A  501          0        19.30                     
CISPEP   4 TRP A  648    PRO A  649          0        -6.27                     
CISPEP   5 SER C  373    PRO C  374          0       -12.40                     
CISPEP   6 PRO C  374    SER C  375          0       -19.73                     
CISPEP   7 ARG C  499    LYS C  500          0        13.38                     
CISPEP   8 LYS C  500    SER C  501          0        18.62                     
CISPEP   9 TRP C  648    PRO C  649          0        -7.08                     
SITE     1 AC1  4 THR A 112  SER A 161  AOV A1001  HOH A2010                    
SITE     1 AC2 21 ASN A  53  ARG A  56  TYR A  61  GLU A 106                    
SITE     2 AC2 21 SER A 107  GLY A 108  ALA A 109  GLY A 110                    
SITE     3 AC2 21 LYS A 111  THR A 112  GLU A 113  ASN A 157                    
SITE     4 AC2 21 ASN A 159  SER A 160  SER A 161  TYR A 388                    
SITE     5 AC2 21 GLY A 389   MG A1000  HOH A2010  HOH A2011                    
SITE     6 AC2 21 HOH A2056                                                     
SITE     1 AC3  5 THR C 112  SER C 161  AOV C1001  HOH C2019                    
SITE     2 AC3  5 HOH C2021                                                     
SITE     1 AC4 23 ASN C  53  ARG C  56  TYR C  61  GLU C 106                    
SITE     2 AC4 23 SER C 107  GLY C 108  ALA C 109  GLY C 110                    
SITE     3 AC4 23 LYS C 111  THR C 112  GLU C 113  ASN C 157                    
SITE     4 AC4 23 ASN C 159  SER C 160  SER C 161  TYR C 388                    
SITE     5 AC4 23 GLY C 389   MG C1000  HOH C2008  HOH C2019                    
SITE     6 AC4 23 HOH C2021  HOH C2055  HOH C2083                               
SITE     1 AC5  4 ASP D  94  ASP D  96  ASN D  98  TYR D 100                    
CRYST1   59.580  158.450  114.340  90.00  91.56  90.00 P 1 21 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      0.016784  0.000000  0.000457        0.00000                         
SCALE2      0.000000  0.006311  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008749        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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