GenomeNet

Database: PDB
Entry: 4LX2
LinkDB: 4LX2
Original site: 4LX2 
HEADER    CONTRACTILE PROTEIN/PROTEIN TRANSPORT   29-JUL-13   4LX2              
TITLE     CRYSTAL STRUCTURE OF MYO5A GLOBULAR TAIL DOMAIN IN COMPLEX WITH       
TITLE    2 MELANOPHILIN GTBD                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCONVENTIONAL MYOSIN-VA;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DILUTE DOMAIN RESIDUES 1464-1855;                          
COMPND   5 SYNONYM: DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE, MYOSIN HEAVY CHAIN   
COMPND   6 12, MYOSIN-12, MYOXIN;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MELANOPHILIN;                                              
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 176-201;                                      
COMPND  12 SYNONYM: EXOPHILIN-3, LEADEN PROTEIN, SLP HOMOLOG LACKING C2 DOMAINS 
COMPND  13 A, SLAC2-A, SYNAPTOTAGMIN-LIKE PROTEIN 2A;                           
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MYO5A, MYH12;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 OTHER_DETAILS: SYNTHESIZED                                           
KEYWDS    DIL, CONTRACTILE PROTEIN-PROTEIN TRANSPORT COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.PYLYPENKO,W.ATTANDA,C.GAUQUELIN,A.HOUDUSSE                          
REVDAT   4   20-SEP-23 4LX2    1       REMARK                                   
REVDAT   3   15-JAN-14 4LX2    1       JRNL                                     
REVDAT   2   18-DEC-13 4LX2    1       JRNL                                     
REVDAT   1   20-NOV-13 4LX2    0                                                
JRNL        AUTH   O.PYLYPENKO,W.ATTANDA,C.GAUQUELIN,M.LAHMANI,D.COULIBALY,     
JRNL        AUTH 2 B.BARON,S.HOOS,M.A.TITUS,P.ENGLAND,A.M.HOUDUSSE              
JRNL        TITL   STRUCTURAL BASIS OF MYOSIN V RAB GTPASE-DEPENDENT CARGO      
JRNL        TITL 2 RECOGNITION.                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 20443 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24248336                                                     
JRNL        DOI    10.1073/PNAS.1314329110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 64346                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3219                            
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 35.5818 -  4.2635    0.99     2785   147  0.1805 0.1922        
REMARK   3     2  4.2635 -  3.3849    1.00     2696   142  0.1434 0.1791        
REMARK   3     3  3.3849 -  2.9573    0.99     2686   142  0.1519 0.2095        
REMARK   3     4  2.9573 -  2.6870    1.00     2682   141  0.1549 0.1745        
REMARK   3     5  2.6870 -  2.4945    1.00     2672   140  0.1499 0.2046        
REMARK   3     6  2.4945 -  2.3474    1.00     2670   141  0.1461 0.1685        
REMARK   3     7  2.3474 -  2.2299    0.99     2671   140  0.1481 0.1836        
REMARK   3     8  2.2299 -  2.1328    0.99     2653   140  0.1491 0.1582        
REMARK   3     9  2.1328 -  2.0507    0.99     2613   138  0.1552 0.1789        
REMARK   3    10  2.0507 -  1.9800    0.99     2630   138  0.1537 0.1810        
REMARK   3    11  1.9800 -  1.9181    1.00     2663   140  0.1557 0.1846        
REMARK   3    12  1.9181 -  1.8632    0.99     2623   138  0.1599 0.2063        
REMARK   3    13  1.8632 -  1.8142    0.99     2674   141  0.1697 0.1912        
REMARK   3    14  1.8142 -  1.7699    1.00     2644   139  0.1867 0.2294        
REMARK   3    15  1.7699 -  1.7297    1.00     2628   138  0.1890 0.2666        
REMARK   3    16  1.7297 -  1.6929    1.00     2647   140  0.1963 0.2145        
REMARK   3    17  1.6929 -  1.6590    1.00     2655   140  0.2084 0.2664        
REMARK   3    18  1.6590 -  1.6277    1.00     2643   139  0.2100 0.2448        
REMARK   3    19  1.6277 -  1.5986    1.00     2639   139  0.2284 0.2745        
REMARK   3    20  1.5986 -  1.5715    1.00     2652   139  0.2432 0.3040        
REMARK   3    21  1.5715 -  1.5462    1.00     2636   139  0.2490 0.2953        
REMARK   3    22  1.5462 -  1.5224    1.00     2627   139  0.2556 0.2700        
REMARK   3    23  1.5224 -  1.5000    1.00     2638   139  0.2846 0.3002        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 56.18                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.99410                                              
REMARK   3    B22 (A**2) : 0.45470                                              
REMARK   3    B33 (A**2) : -1.44880                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.31600                                             
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      :  0.011           3145                                  
REMARK   3   ANGLE     :  1.279           4274                                  
REMARK   3   CHIRALITY :  0.070            494                                  
REMARK   3   PLANARITY :  0.006            546                                  
REMARK   3   DIHEDRAL  : 13.269           1220                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESSEQ 1470:1853))                     
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4579 -20.5130 -16.7305              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0601 T22:   0.0943                                     
REMARK   3      T33:   0.1121 T12:   0.0226                                     
REMARK   3      T13:   0.0078 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6431 L22:   0.7609                                     
REMARK   3      L33:   2.3215 L12:   0.4225                                     
REMARK   3      L13:   0.6979 L23:   0.6861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:  -0.0541 S13:   0.0411                       
REMARK   3      S21:  -0.0484 S22:  -0.0154 S23:   0.0298                       
REMARK   3      S31:   0.0357 S32:  -0.0475 S33:  -0.0192                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESSEQ 185:191))                       
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7768 -46.6486 -34.7343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6939 T22:   0.1588                                     
REMARK   3      T33:   0.3271 T12:   0.0419                                     
REMARK   3      T13:  -0.0226 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8616 L22:   5.8436                                     
REMARK   3      L33:   1.5858 L12:   1.0333                                     
REMARK   3      L13:  -0.1815 L23:   0.1955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0791 S12:   0.0156 S13:  -0.1245                       
REMARK   3      S21:  -0.0906 S22:   0.0161 S23:  -0.1628                       
REMARK   3      S31:   0.5039 S32:  -0.0476 S33:  -0.0999                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESSEQ 192:196))                       
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5360 -41.9858 -32.6243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7434 T22:   0.5341                                     
REMARK   3      T33:   0.8151 T12:   0.2611                                     
REMARK   3      T13:   0.0527 T23:  -0.1139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8539 L22:   6.3999                                     
REMARK   3      L33:   1.2418 L12:  -5.5377                                     
REMARK   3      L13:  -2.4225 L23:   2.8157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2679 S12:  -0.0704 S13:  -0.8390                       
REMARK   3      S21:  -0.0401 S22:   0.1089 S23:  -0.3643                       
REMARK   3      S31:   1.1176 S32:   0.5291 S33:  -0.3696                       
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 4LX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081193.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980110                           
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64638                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4LX0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MPD, PH 8, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.93500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.55500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.93500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.55500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A  1462                                                      
REMARK 465     ASN A  1463                                                      
REMARK 465     ILE A  1464                                                      
REMARK 465     PRO A  1465                                                      
REMARK 465     ARG A  1466                                                      
REMARK 465     LYS A  1467                                                      
REMARK 465     GLU A  1468                                                      
REMARK 465     LYS A  1469                                                      
REMARK 465     THR A  1632                                                      
REMARK 465     ILE A  1633                                                      
REMARK 465     GLN A  1634                                                      
REMARK 465     GLY A  1635                                                      
REMARK 465     VAL A  1636                                                      
REMARK 465     SER A  1637                                                      
REMARK 465     GLY A  1638                                                      
REMARK 465     VAL A  1639                                                      
REMARK 465     LYS A  1640                                                      
REMARK 465     PRO A  1641                                                      
REMARK 465     THR A  1642                                                      
REMARK 465     GLY A  1643                                                      
REMARK 465     LEU A  1644                                                      
REMARK 465     ARG A  1645                                                      
REMARK 465     LYS A  1646                                                      
REMARK 465     ARG A  1647                                                      
REMARK 465     THR A  1648                                                      
REMARK 465     SER A  1649                                                      
REMARK 465     SER A  1650                                                      
REMARK 465     ILE A  1651                                                      
REMARK 465     ALA A  1652                                                      
REMARK 465     ASP A  1653                                                      
REMARK 465     GLU A  1654                                                      
REMARK 465     ARG B   176                                                      
REMARK 465     ASP B   177                                                      
REMARK 465     GLN B   178                                                      
REMARK 465     PRO B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     ASN B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     LYS B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ASP B   199                                                      
REMARK 465     SER B   200                                                      
REMARK 465     ASP B   201                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A1479    NZ                                                  
REMARK 470     LYS A1484    NZ                                                  
REMARK 470     LYS A1494    CE   NZ                                             
REMARK 470     LEU A1502    CG   CD1  CD2                                       
REMARK 470     GLU A1572    OE2                                                 
REMARK 470     GLU A1573    CD   OE1  OE2                                       
REMARK 470     LEU A1615    CG   CD1  CD2                                       
REMARK 470     ARG A1664    CD   NE   CZ   NH1  NH2                             
REMARK 470     MET A1715    CE                                                  
REMARK 470     GLU A1726    OE2                                                 
REMARK 470     LYS A1739    CD   CE   NZ                                        
REMARK 470     VAL A1787    CG1  CG2                                            
REMARK 470     LYS A1810    CG   CD   CE   NZ                                   
REMARK 470     ASP A1811    OD1                                                 
REMARK 470     GLN A1814    CD   OE1  NE2                                       
REMARK 470     LYS B 185    CG   CD   CE   NZ                                   
REMARK 470     ARG B 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 193    CG   OD1  OD2                                       
REMARK 470     VAL B 194    CG1  CG2                                            
REMARK 470     ASP B 195    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A1490      -62.74   -128.19                                   
REMARK 500    CYS A1769       53.49    -98.37                                   
REMARK 500    ASN A1788     -166.85   -161.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPE A 1901                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1901                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LWZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LX0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LX1   RELATED DB: PDB                                   
DBREF  4LX2 A 1462  1853  UNP    Q9Y4I1   MYO5A_HUMAN   1464   1855             
DBREF  4LX2 B  176   201  UNP    Q91V27   MELPH_MOUSE    176    201             
SEQRES   1 A  392  VAL ASN ILE PRO ARG LYS GLU LYS ASP PHE GLN GLY MET          
SEQRES   2 A  392  LEU GLU TYR LYS LYS GLU ASP GLU GLN LYS LEU VAL LYS          
SEQRES   3 A  392  ASN LEU ILE LEU GLU LEU LYS PRO ARG GLY VAL ALA VAL          
SEQRES   4 A  392  ASN LEU ILE PRO GLY LEU PRO ALA TYR ILE LEU PHE MET          
SEQRES   5 A  392  CYS VAL ARG HIS ALA ASP TYR LEU ASN ASP ASP GLN LYS          
SEQRES   6 A  392  VAL ARG SER LEU LEU THR SER THR ILE ASN SER ILE LYS          
SEQRES   7 A  392  LYS VAL LEU LYS LYS ARG GLY ASP ASP PHE GLU THR VAL          
SEQRES   8 A  392  SER PHE TRP LEU SER ASN THR CYS ARG PHE LEU HIS CYS          
SEQRES   9 A  392  LEU LYS GLN TYR SER GLY GLU GLU GLY PHE MET LYS HIS          
SEQRES  10 A  392  ASN THR SER ARG GLN ASN GLU HIS CYS LEU THR ASN PHE          
SEQRES  11 A  392  ASP LEU ALA GLU TYR ARG GLN VAL LEU SER ASP LEU ALA          
SEQRES  12 A  392  ILE GLN ILE TYR GLN GLN LEU VAL ARG VAL LEU GLU ASN          
SEQRES  13 A  392  ILE LEU GLN PRO MET ILE VAL SER GLY MET LEU GLU HIS          
SEQRES  14 A  392  GLU THR ILE GLN GLY VAL SER GLY VAL LYS PRO THR GLY          
SEQRES  15 A  392  LEU ARG LYS ARG THR SER SER ILE ALA ASP GLU GLY THR          
SEQRES  16 A  392  TYR THR LEU ASP SER ILE LEU ARG GLN LEU ASN SER PHE          
SEQRES  17 A  392  HIS SER VAL MET CYS GLN HIS GLY MET ASP PRO GLU LEU          
SEQRES  18 A  392  ILE LYS GLN VAL VAL LYS GLN MET PHE TYR ILE ILE GLY          
SEQRES  19 A  392  ALA ILE THR LEU ASN ASN LEU LEU LEU ARG LYS ASP MET          
SEQRES  20 A  392  CYS SER TRP SER LYS GLY MET GLN ILE ARG TYR ASN VAL          
SEQRES  21 A  392  SER GLN LEU GLU GLU TRP LEU ARG ASP LYS ASN LEU MET          
SEQRES  22 A  392  ASN SER GLY ALA LYS GLU THR LEU GLU PRO LEU ILE GLN          
SEQRES  23 A  392  ALA ALA GLN LEU LEU GLN VAL LYS LYS LYS THR ASP ASP          
SEQRES  24 A  392  ASP ALA GLU ALA ILE CYS SER MET CYS ASN ALA LEU THR          
SEQRES  25 A  392  THR ALA GLN ILE VAL LYS VAL LEU ASN LEU TYR THR PRO          
SEQRES  26 A  392  VAL ASN GLU PHE GLU GLU ARG VAL SER VAL SER PHE ILE          
SEQRES  27 A  392  ARG THR ILE GLN MET ARG LEU ARG ASP ARG LYS ASP SER          
SEQRES  28 A  392  PRO GLN LEU LEU MET ASP ALA LYS HIS ILE PHE PRO VAL          
SEQRES  29 A  392  THR PHE PRO PHE ASN PRO SER SER LEU ALA LEU GLU THR          
SEQRES  30 A  392  ILE GLN ILE PRO ALA SER LEU GLY LEU GLY PHE ILE SER          
SEQRES  31 A  392  ARG VAL                                                      
SEQRES   1 B   26  ARG ASP GLN PRO LEU ASN SER LYS LYS LYS LYS ARG LEU          
SEQRES   2 B   26  LEU SER PHE ARG ASP VAL ASP PHE GLU GLU ASP SER ASP          
HET    EPE  A1901      10                                                       
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   3  EPE    C8 H18 N2 O4 S                                               
FORMUL   4  HOH   *436(H2 O)                                                    
HELIX    1   1 LYS A 1478  GLU A 1480  5                                   3    
HELIX    2   2 ASP A 1481  ILE A 1490  1                                  10    
HELIX    3   3 GLY A 1497  ASN A 1501  5                                   5    
HELIX    4   4 GLY A 1505  LEU A 1521  1                                  17    
HELIX    5   5 ASP A 1523  GLY A 1546  1                                  24    
HELIX    6   6 ASP A 1548  TYR A 1569  1                                  22    
HELIX    7   7 GLU A 1572  MET A 1576  5                                   5    
HELIX    8   8 THR A 1580  GLU A 1585  1                                   6    
HELIX    9   9 LEU A 1593  GLN A 1620  1                                  28    
HELIX   10  10 MET A 1622  LEU A 1628  1                                   7    
HELIX   11  11 THR A 1658  HIS A 1676  1                                  19    
HELIX   12  12 ASP A 1679  ARG A 1705  1                                  27    
HELIX   13  13 SER A 1710  LYS A 1731  1                                  22    
HELIX   14  14 GLY A 1737  LEU A 1742  1                                   6    
HELIX   15  15 LEU A 1742  VAL A 1754  1                                  13    
HELIX   16  16 THR A 1758  CYS A 1769  1                                  12    
HELIX   17  17 THR A 1773  TYR A 1784  1                                  12    
HELIX   18  18 SER A 1795  LEU A 1806  1                                  12    
HELIX   19  19 ALA A 1835  ILE A 1839  5                                   5    
HELIX   20  20 PRO A 1842  GLY A 1846  5                                   5    
HELIX   21  21 ARG B  192  PHE B  196  5                                   5    
SHEET    1   A 2 MET A1474  GLU A1476  0                                        
SHEET    2   A 2 SER A1851  VAL A1853 -1  O  SER A1851   N  GLU A1476           
SHEET    1   B 2 PHE A1591  ASP A1592  0                                        
SHEET    2   B 2 ARG B 187  LEU B 188  1  O  ARG B 187   N  ASP A1592           
SITE     1 AC1  6 PHE A1471  ASN A1522  ASP A1523  ASP A1524                    
SITE     2 AC1  6 GLN A1525  HOH A2195                                          
CRYST1   99.870   41.110  109.580  90.00 115.63  90.00 C 1 2 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      0.010013  0.000000  0.004804        0.00000                         
SCALE2      0.000000  0.024325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010122        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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