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Database: PDB
Entry: 3PZD
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Original site: 3PZD 
HEADER    MOTOR PROTEIN/APOPTOSIS                 14-DEC-10   3PZD              
TITLE     STRUCTURE OF THE MYOSIN X MYTH4-FERM/DCC COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN-X;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MYTH4-FERM TANDEM;                                         
COMPND   5 SYNONYM: UNCONVENTIONAL MYOSIN-10;                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NETRIN RECEPTOR DCC;                                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: P3 MOTIF;                                                  
COMPND  11 SYNONYM: TUMOR SUPPRESSOR PROTEIN DCC;                               
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 GENE: KIAA0799, MYO10;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: DCC;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-PROTEIN COMPLEX, MYTH4 DOMAIN, FERM DOMAIN, CARGO BINDING,    
KEYWDS   2 MOTOR PROTEIN-APOPTOSIS COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.WEI,J.YAN,L.PAN,M.ZHANG                                             
REVDAT   2   04-SEP-13 3PZD    1       JRNL   VERSN                             
REVDAT   1   23-FEB-11 3PZD    0                                                
JRNL        AUTH   Z.WEI,J.YAN,Q.LU,L.PAN,M.ZHANG                               
JRNL        TITL   CARGO RECOGNITION MECHANISM OF MYOSIN X REVEALED BY THE      
JRNL        TITL 2 STRUCTURE OF ITS TAIL MYTH4-FERM TANDEM IN COMPLEX WITH THE  
JRNL        TITL 3 DCC P3 DOMAIN                                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  3572 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21321230                                                     
JRNL        DOI    10.1073/PNAS.1016567108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 23737                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1243                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1694                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4220                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 101                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.38000                                              
REMARK   3    B22 (A**2) : 0.69000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.09000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.282         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.202         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.778        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4319 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5849 ; 1.145 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   530 ; 5.625 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   193 ;36.714 ;24.560       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   750 ;17.668 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;15.772 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   653 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3239 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2666 ; 1.456 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4294 ; 2.552 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1653 ; 4.017 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1555 ; 5.872 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1501        A  1696                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9224   0.1997  13.4541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0670 T22:   0.0086                                     
REMARK   3      T33:   0.0106 T12:  -0.0048                                     
REMARK   3      T13:  -0.0221 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3376 L22:   3.4258                                     
REMARK   3      L33:   1.9144 L12:  -0.5145                                     
REMARK   3      L13:   0.2661 L23:   0.3366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0729 S12:   0.0676 S13:   0.1283                       
REMARK   3      S21:  -0.2681 S22:   0.0336 S23:   0.1248                       
REMARK   3      S31:  -0.1053 S32:   0.0090 S33:   0.0393                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1697        A  1789                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0484   4.7247  17.3242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1254 T22:   0.1933                                     
REMARK   3      T33:   0.1070 T12:  -0.0339                                     
REMARK   3      T13:   0.0369 T23:  -0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1763 L22:   1.4316                                     
REMARK   3      L33:   3.5511 L12:   1.6005                                     
REMARK   3      L13:   2.3407 L23:   1.7538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1910 S12:   0.3873 S13:   0.2002                       
REMARK   3      S21:  -0.0622 S22:   0.1695 S23:  -0.1386                       
REMARK   3      S31:  -0.2538 S32:   0.3807 S33:   0.0214                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1790        A  1952                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.5821  13.5653  15.1523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1340 T22:   0.1462                                     
REMARK   3      T33:   0.1414 T12:   0.0275                                     
REMARK   3      T13:   0.0147 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2404 L22:   1.1261                                     
REMARK   3      L33:   4.9349 L12:  -0.1729                                     
REMARK   3      L13:  -2.5883 L23:   0.7979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4333 S12:   0.0529 S13:   0.6459                       
REMARK   3      S21:   0.0730 S22:  -0.1098 S23:  -0.1168                       
REMARK   3      S31:  -0.6564 S32:  -0.1139 S33:  -0.3234                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1953        A  2047                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8220  21.8984  34.4471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4262 T22:   0.3676                                     
REMARK   3      T33:   0.3432 T12:   0.0025                                     
REMARK   3      T13:   0.1392 T23:  -0.1545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1364 L22:   6.4848                                     
REMARK   3      L33:   5.7988 L12:  -0.4380                                     
REMARK   3      L13:  -1.2687 L23:   0.8237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4062 S12:  -0.2002 S13:   1.0485                       
REMARK   3      S21:   0.1962 S22:  -0.0084 S23:   0.0346                       
REMARK   3      S31:  -1.1786 S32:  -0.3321 S33:  -0.3979                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1407        B  1443                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.6597  13.4084  47.7273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4472 T22:   0.5376                                     
REMARK   3      T33:   0.3543 T12:  -0.0539                                     
REMARK   3      T13:   0.0400 T23:  -0.1695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8401 L22:   1.8164                                     
REMARK   3      L33:   9.7333 L12:   1.7113                                     
REMARK   3      L13:   5.2760 L23:   0.7842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4380 S12:  -0.0820 S13:  -0.5602                       
REMARK   3      S21:   0.0997 S22:   0.1027 S23:  -0.3042                       
REMARK   3      S31:   0.6193 S32:  -0.4536 S33:  -0.5408                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES                                                  
REMARK   4                                                                      
REMARK   4 3PZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB062999.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24981                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 10% GLYCEROL, HEPES         
REMARK 280  BUFFER, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K     
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       24.76400            
REMARK 290   SMTRY3   2  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: 1650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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     ILE A  1900                                                      
REMARK 465     SER A  1901                                                      
REMARK 465     GLN A  1902                                                      
REMARK 465     SER A  1903                                                      
REMARK 465     THR A  1904                                                      
REMARK 465     LYS A  1905                                                      
REMARK 465     THR A  1906                                                      
REMARK 465     GLN A  1907                                                      
REMARK 465     MET A  1908                                                      
REMARK 465     LEU A  1909                                                      
REMARK 465     GLU A  1964                                                      
REMARK 465     GLY A  1965                                                      
REMARK 465     GLY A  1966                                                      
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     ARG A1731    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1736    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1739    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A1858    CG   CD   OE1  NE2                                  
REMARK 470     ASP A1910    CG   OD1  OD2                                       
REMARK 470     MET A1911    CG   SD   CE                                        
REMARK 470     TRP A1912    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1912    CZ3  CH2                                            
REMARK 470     ILE A1913    CG1  CG2  CD1                                       
REMARK 470     LYS A1914    CG   CD   CE   NZ                                   
REMARK 470     GLU A1937    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1969    CG   CD   OE1  NE2                                  
REMARK 470     LYS A2011    CG   CD   CE   NZ                                   
REMARK 470     GLU A2016    CG   CD   OE1  OE2                                  
REMARK 470     LEU A2020    CG   CD1  CD2                                       
REMARK 470     ARG A2044    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B1408    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B1416    OG                                                  
REMARK 470     LEU B1423    CG   CD1  CD2                                       
REMARK 470     GLU B1425    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1426    CG   CD   OE1  NE2                                  
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    LEU A1557   CA  -  CB  -  CG  ANGL. DEV. =  17.3 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    SER A1581       62.48   -108.58                                   
REMARK 500    LYS A1680     -116.66   -111.20                                   
REMARK 500    HIS A1750      -68.06   -138.68                                   
REMARK 500    ASP A1793      102.44   -162.71                                   
REMARK 500    PRO A1850      132.53    -39.60                                   
REMARK 500    CYS A1962      -74.44   -100.05                                   
REMARK 500    ARG A1985      109.66    -49.09                                   
REMARK 500    ASN A2008       69.37     21.49                                   
REMARK 500    ASP A2015      118.59    -34.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A 1747     ASN A 1748                  149.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1                   
DBREF  3PZD A 1503  2047  UNP    Q9HD67   MYO10_HUMAN   1503   2047             
DBREF  3PZD B 1408  1443  UNP    P70211   DCC_MOUSE     1410   1445             
SEQADV 3PZD GLU A 1501  UNP  Q9HD67              EXPRESSION TAG                 
SEQADV 3PZD PHE A 1502  UNP  Q9HD67              EXPRESSION TAG                 
SEQADV 3PZD     A       UNP  Q9HD67    PHE  1871 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    THR  1872 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    PRO  1873 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    CYS  1874 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1875 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1876 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    LEU  1877 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1878 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    LYS  1879 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1880 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1881 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    THR  1882 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    SER  1883 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    PHE  1884 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    LEU  1885 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1886 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLY  1887 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    THR  1888 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    LEU  1889 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1890 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1891 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    SER  1892 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    PHE  1893 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1894 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    THR  1895 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLY  1896 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    SER  1897 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    VAL  1898 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    VAL  1899 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    ARG  1900 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLN  1901 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    LYS  1902 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    VAL  1903 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1904 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1905 DELETION                       
SEQADV 3PZD     A       UNP  Q9HD67    GLU  1906 DELETION                       
SEQRES   1 A  511  GLU PHE ASP THR PRO THR GLN GLN LEU ILE GLN ASP ILE          
SEQRES   2 A  511  LYS GLU ASN CYS LEU ASN SER ASP VAL VAL GLU GLN ILE          
SEQRES   3 A  511  TYR LYS ARG ASN PRO ILE LEU ARG TYR THR HIS HIS PRO          
SEQRES   4 A  511  LEU HIS SER PRO LEU LEU PRO LEU PRO TYR GLY ASP ILE          
SEQRES   5 A  511  ASN LEU ASN LEU LEU LYS ASP LYS GLY TYR THR THR LEU          
SEQRES   6 A  511  GLN ASP GLU ALA ILE LYS ILE PHE ASN SER LEU GLN GLN          
SEQRES   7 A  511  LEU GLU SER MET SER ASP PRO ILE PRO ILE ILE GLN GLY          
SEQRES   8 A  511  ILE LEU GLN THR GLY HIS ASP LEU ARG PRO LEU ARG ASP          
SEQRES   9 A  511  GLU LEU TYR CYS GLN LEU ILE LYS GLN THR ASN LYS VAL          
SEQRES  10 A  511  PRO HIS PRO GLY SER VAL GLY ASN LEU TYR SER TRP GLN          
SEQRES  11 A  511  ILE LEU THR CYS LEU SER CYS THR PHE LEU PRO SER ARG          
SEQRES  12 A  511  GLY ILE LEU LYS TYR LEU LYS PHE HIS LEU LYS ARG ILE          
SEQRES  13 A  511  ARG GLU GLN PHE PRO GLY SER GLU MET GLU LYS TYR ALA          
SEQRES  14 A  511  LEU PHE THR TYR GLU SER LEU LYS LYS THR LYS CYS ARG          
SEQRES  15 A  511  GLU PHE VAL PRO SER ARG ASP GLU ILE GLU ALA LEU ILE          
SEQRES  16 A  511  HIS ARG GLN GLU MET THR SER THR VAL TYR CYS HIS GLY          
SEQRES  17 A  511  GLY GLY SER CYS LYS ILE THR ILE ASN SER HIS THR THR          
SEQRES  18 A  511  ALA GLY GLU VAL VAL GLU LYS LEU ILE ARG GLY LEU ALA          
SEQRES  19 A  511  MET GLU ASP SER ARG ASN MET PHE ALA LEU PHE GLU TYR          
SEQRES  20 A  511  ASN GLY HIS VAL ASP LYS ALA ILE GLU SER ARG THR VAL          
SEQRES  21 A  511  VAL ALA ASP VAL LEU ALA LYS PHE GLU LYS LEU ALA ALA          
SEQRES  22 A  511  THR SER GLU VAL GLY ASP LEU PRO TRP LYS PHE TYR PHE          
SEQRES  23 A  511  LYS LEU TYR CYS PHE LEU ASP THR ASP ASN VAL PRO LYS          
SEQRES  24 A  511  ASP SER VAL GLU PHE ALA PHE MET PHE GLU GLN ALA HIS          
SEQRES  25 A  511  GLU ALA VAL ILE HIS GLY HIS HIS PRO ALA PRO GLU GLU          
SEQRES  26 A  511  ASN LEU GLN VAL LEU ALA ALA LEU ARG LEU GLN TYR LEU          
SEQRES  27 A  511  GLN GLY ASP TYR THR LEU HIS ALA ALA ILE PRO PRO LEU          
SEQRES  28 A  511  GLU GLU VAL TYR SER LEU GLN ARG LEU LYS ALA ARG ILE          
SEQRES  29 A  511  SER GLN SER THR LYS THR GLN MET LEU ASP MET TRP ILE          
SEQRES  30 A  511  LYS GLU GLU VAL SER SER ALA ARG ALA SER ILE ILE ASP          
SEQRES  31 A  511  LYS TRP ARG LYS PHE GLN GLY MET ASN GLN GLU GLN ALA          
SEQRES  32 A  511  MET ALA LYS TYR MET ALA LEU ILE LYS GLU TRP PRO GLY          
SEQRES  33 A  511  TYR GLY SER THR LEU PHE ASP VAL GLU CYS LYS GLU GLY          
SEQRES  34 A  511  GLY PHE PRO GLN GLU LEU TRP LEU GLY VAL SER ALA ASP          
SEQRES  35 A  511  ALA VAL SER VAL TYR LYS ARG GLY GLU GLY ARG PRO LEU          
SEQRES  36 A  511  GLU VAL PHE GLN TYR GLU HIS ILE LEU SER PHE GLY ALA          
SEQRES  37 A  511  PRO LEU ALA ASN THR TYR LYS ILE VAL VAL ASP GLU ARG          
SEQRES  38 A  511  GLU LEU LEU PHE GLU THR SER GLU VAL VAL ASP VAL ALA          
SEQRES  39 A  511  LYS LEU MET LYS ALA TYR ILE SER MET ILE VAL LYS LYS          
SEQRES  40 A  511  ARG TYR SER THR                                              
SEQRES   1 B   36  HIS LYS PRO THR GLU ASP PRO ALA SER VAL TYR GLU GLN          
SEQRES   2 B   36  ASP ASP LEU SER GLU GLN MET ALA SER LEU GLU GLY LEU          
SEQRES   3 B   36  MET LYS GLN LEU ASN ALA ILE THR GLY SER                      
HET    GOL  A   1       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *101(H2 O)                                                    
HELIX    1   1 THR A 1504  GLU A 1515  1                                  12    
HELIX    2   2 ASN A 1519  ASN A 1530  1                                  12    
HELIX    3   3 PRO A 1531  ARG A 1534  5                                   4    
HELIX    4   4 ASN A 1553  LYS A 1560  1                                   8    
HELIX    5   5 THR A 1564  GLU A 1580  1                                  17    
HELIX    6   6 PRO A 1585  LEU A 1599  1                                  15    
HELIX    7   7 PRO A 1601  THR A 1614  1                                  14    
HELIX    8   8 SER A 1622  SER A 1636  1                                  15    
HELIX    9   9 SER A 1642  PHE A 1660  1                                  19    
HELIX   10  10 SER A 1663  LYS A 1677  1                                  15    
HELIX   11  11 SER A 1687  HIS A 1696  1                                  10    
HELIX   12  12 THR A 1721  LEU A 1733  1                                  13    
HELIX   13  13 VAL A 1760  ALA A 1772  1                                  13    
HELIX   14  14 SER A 1801  GLY A 1818  1                                  18    
HELIX   15  15 PRO A 1823  GLY A 1840  1                                  18    
HELIX   16  16 PRO A 1850  VAL A 1854  5                                   5    
HELIX   17  17 LEU A 1857  ALA A 1862  1                                   6    
HELIX   18  18 ASP A 1910  LYS A 1930  1                                  21    
HELIX   19  19 ASN A 1935  LYS A 1948  1                                  14    
HELIX   20  20 GLU A 2025  SER A 2046  1                                  22    
HELIX   21  21 ASP B 1413  GLN B 1420  1                                   8    
HELIX   22  22 ASP B 1422  GLY B 1442  1                                  21    
SHEET    1   A 5 SER A1711  ILE A1716  0                                        
SHEET    2   A 5 MET A1700  TYR A1705 -1  N  VAL A1704   O  CYS A1712           
SHEET    3   A 5 LYS A1783  CYS A1790  1  O  PHE A1784   N  TYR A1705           
SHEET    4   A 5 MET A1741  TYR A1747 -1  N  MET A1741   O  TYR A1789           
SHEET    5   A 5 ASP A1752  ALA A1754 -1  O  LYS A1753   N  GLU A1746           
SHEET    1   B 4 THR A1956  GLU A1961  0                                        
SHEET    2   B 4 GLU A1970  VAL A1975 -1  O  LEU A1973   N  PHE A1958           
SHEET    3   B 4 ALA A1979  LYS A1984 -1  O  SER A1981   N  GLY A1974           
SHEET    4   B 4 GLU A1992  GLN A1995 -1  O  PHE A1994   N  VAL A1980           
SHEET    1   C 3 ILE A1999  GLY A2003  0                                        
SHEET    2   C 3 THR A2009  VAL A2014 -1  O  LYS A2011   N  GLY A2003           
SHEET    3   C 3 ARG A2017  GLU A2022 -1  O  PHE A2021   N  TYR A2010           
SITE     1 AC1  6 CYS A1706  HIS A1707  GLY A1708  ALA A1805                    
SITE     2 AC1  6 PHE A1806  GLU A1809                                          
CRYST1   85.167   49.528   92.814  90.00 112.58  90.00 P 1 21 1      2          
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      0.011742  0.000000  0.004883        0.00000                         
SCALE2      0.000000  0.020191  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011669        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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