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Database: PDB
Entry: 2Y0M
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Original site: 2Y0M 
HEADER    TRANSCRIPTION                           03-DEC-10   2Y0M              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE                       
TITLE    2 COMPENSATION FACTORS MSL1 AND MOF                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HISTONE ACETYLTRANSFERASE MYST1;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HAT DOMAIN, RESIDUES 174-458;                              
COMPND   5 SYNONYM: MYST-1, MOZ, YBF2/SAS3, SAS2 AND TIP60 PROTEIN 1, HMOF;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MALE-SPECIFIC LETHAL 1 HOMOLOG;                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: PEHE DOMAIN, RESIDUES 470-540;                             
COMPND  11 SYNONYM: MSL-1, HAMPIN, MALE-SPECIFIC LETHAL 1-LIKE 1, MSL1-LIKE 1,  
COMPND  12  MALE-SPECIFIC LETHAL-1 HOMOLOG 1, MSL1;                             
COMPND  13 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: ESCHERICHA COLI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PRSFDUET-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHA COLI;                                  
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PPROEXHTB                                  
KEYWDS    TRANSCRIPTION, CHROMATIN, X CHROMOSOME, MSL COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KADLEC,E.HALLACLI,M.LIPP,H.HOLZ,J.SANCHEZ WEATHERBY,S.CUSACK,       
AUTHOR   2 A.AKHTAR                                                             
REVDAT   2   16-FEB-11 2Y0M    1       JRNL                                     
REVDAT   1   12-JAN-11 2Y0M    0                                                
JRNL        AUTH   J.KADLEC,E.HALLACLI,M.LIPP,H.HOLZ,J.SANCHEZ-WEATHERBY,       
JRNL        AUTH 2 S.CUSACK,A.AKHTAR                                            
JRNL        TITL   STRUCTURAL BASIS FOR MOF AND MSL3 RECRUITMENT INTO THE       
JRNL        TITL 2 DOSAGE COMPENSATION COMPLEX BY MSL1.                         
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   142 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21217699                                                     
JRNL        DOI    10.1038/NSMB.1960                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0085                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.03                          
REMARK   3   NUMBER OF REFLECTIONS             : 17596                          
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) : 0.22477                         
REMARK   3   R VALUE            (WORKING SET) : 0.22316                         
REMARK   3   FREE R VALUE                     : 0.25587                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 946                             
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) : 2.699                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.768                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1229                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.304                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.249                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.031                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 18.55                                                
REMARK   3    B22 (A**2) : 18.55                                                
REMARK   3    B33 (A**2) : -37.09                                               
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.224         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.034        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2766 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3742 ; 0.945 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   313 ; 4.921 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   128 ;31.322 ;23.516       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   498 ;15.002 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;14.052 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   390 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2057 ; 0.003 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   177        A   449                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9050 -20.1624  19.7029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1293 T22:   0.1371                                     
REMARK   3      T33:   0.0249 T12:  -0.0818                                     
REMARK   3      T13:  -0.0092 T23:  -0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7501 L22:   3.5069                                     
REMARK   3      L33:   3.2344 L12:  -0.6672                                     
REMARK   3      L13:   0.4091 L23:  -1.1707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0139 S12:  -0.0307 S13:   0.0371                       
REMARK   3      S21:   0.2604 S22:  -0.1386 S23:  -0.0054                       
REMARK   3      S31:  -0.2348 S32:   0.0851 S33:   0.1247                       
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 :   B   495        B   536                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5628  -0.7034  21.0780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4877 T22:   0.2248                                     
REMARK   3      T33:   0.3770 T12:  -0.2988                                     
REMARK   3      T13:   0.0467 T23:  -0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.8995 L22:   2.8318                                     
REMARK   3      L33:  22.3872 L12:  -3.2157                                     
REMARK   3      L13:  15.8069 L23:  -3.8137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0052 S12:  -0.5308 S13:   0.5547                       
REMARK   3      S21:   0.1575 S22:  -0.1033 S23:  -0.2125                       
REMARK   3      S31:  -0.6110 S32:  -0.0575 S33:   0.1085                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2Y0M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46557.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18543                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4                                  
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.05                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.81                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.16                               
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 2GIV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE (PH 5), 1.0         
REMARK 280  M SODIUM FORMATE.                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       90.47000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.37500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.18750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       90.47000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       60.56250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       60.56250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       90.47000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       20.18750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       90.47000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.37500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       90.47000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       40.37500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       90.47000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       60.56250            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       20.18750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       90.47000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       20.18750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       60.56250            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       90.47000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       90.47000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       40.37500            
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 64010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       80.75000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       80.75000            
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   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     THR A   174                                                      
REMARK 465     LYS A   175                                                      
REMARK 465     VAL A   176                                                      
REMARK 465     HIS A   450                                                      
REMARK 465     LYS A   451                                                      
REMARK 465     GLN A   452                                                      
REMARK 465     VAL A   453                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     LEU A   455                                                      
REMARK 465     SER A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     GLY B   467                                                      
REMARK 465     ALA B   468                                                      
REMARK 465     MET B   469                                                      
REMARK 465     GLY B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     THR B   472                                                      
REMARK 465     SER B   473                                                      
REMARK 465     VAL B   474                                                      
REMARK 465     LEU B   475                                                      
REMARK 465     ALA B   476                                                      
REMARK 465     VAL B   477                                                      
REMARK 465     PRO B   478                                                      
REMARK 465     SER B   479                                                      
REMARK 465     TRP B   480                                                      
REMARK 465     ARG B   481                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     HIS B   483                                                      
REMARK 465     SER B   484                                                      
REMARK 465     VAL B   485                                                      
REMARK 465     GLU B   486                                                      
REMARK 465     PRO B   487                                                      
REMARK 465     LEU B   488                                                      
REMARK 465     ARG B   489                                                      
REMARK 465     ASP B   490                                                      
REMARK 465     PRO B   491                                                      
REMARK 465     ASN B   492                                                      
REMARK 465     PRO B   493                                                      
REMARK 465     SER B   494                                                      
REMARK 465     GLN B   537                                                      
REMARK 465     LEU B   538                                                      
REMARK 465     ARG B   539                                                      
REMARK 465     MET B   540                                                      
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    GLU A 199     -132.98     49.69                                   
REMARK 500    SER A 244     -125.53     56.58                                   
REMARK 500    TYR A 277      -35.51   -132.91                                   
REMARK 500    ALA A 315      -62.04   -102.67                                   
REMARK 500    ARG B 535       79.00   -100.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1451  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 210   SG                                                     
REMARK 620 2 HIS A 226   NE2 101.6                                              
REMARK 620 3 CYS A 230   SG  105.5 105.6                                        
REMARK 620 4 CYS A 213   SG  108.9 115.2 118.4                                  
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 ACO A1450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1451                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Y0N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  DOSAGE COMPENSATION FACTORS MSL1 AND MSL3                           
DBREF  2Y0M A  174   458  UNP    Q9H7Z6   MYST1_HUMAN    174    458             
DBREF  2Y0M B  470   540  UNP    Q6PDM1   MSL1_MOUSE     470    540             
SEQADV 2Y0M MET A  172  UNP  Q9H7Z6              EXPRESSION TAG                 
SEQADV 2Y0M GLY A  173  UNP  Q9H7Z6              EXPRESSION TAG                 
SEQADV 2Y0M GLY B  467  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0M ALA B  468  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0M MET B  469  UNP  Q6PDM1              EXPRESSION TAG                 
SEQRES   1 A  287  MET GLY THR LYS VAL LYS TYR VAL ASP LYS ILE HIS ILE          
SEQRES   2 A  287  GLY ASN TYR GLU ILE ASP ALA TRP TYR PHE SER PRO PHE          
SEQRES   3 A  287  PRO GLU ASP TYR GLY LYS GLN PRO LYS LEU TRP LEU CYS          
SEQRES   4 A  287  GLU TYR CYS LEU LYS TYR MET LYS TYR GLU LYS SER TYR          
SEQRES   5 A  287  ARG PHE HIS LEU GLY GLN CYS GLN TRP ARG GLN PRO PRO          
SEQRES   6 A  287  GLY LYS GLU ILE TYR ARG LYS SER ASN ILE SER VAL TYR          
SEQRES   7 A  287  GLU VAL ASP GLY LYS ASP HIS LYS ILE TYR CYS GLN ASN          
SEQRES   8 A  287  LEU CYS LEU LEU ALA LYS LEU PHE LEU ASP HIS ALY THR          
SEQRES   9 A  287  LEU TYR PHE ASP VAL GLU PRO PHE VAL PHE TYR ILE LEU          
SEQRES  10 A  287  THR GLU VAL ASP ARG GLN GLY ALA HIS ILE VAL GLY TYR          
SEQRES  11 A  287  PHE SER LYS GLU LYS GLU SER PRO ASP GLY ASN ASN VAL          
SEQRES  12 A  287  ALA CSO ILE LEU THR LEU PRO PRO TYR GLN ARG ARG GLY          
SEQRES  13 A  287  TYR GLY LYS PHE LEU ILE ALA PHE SER TYR GLU LEU SER          
SEQRES  14 A  287  LYS LEU GLU SER THR VAL GLY SER PRO GLU LYS PRO LEU          
SEQRES  15 A  287  SER ASP LEU GLY LYS LEU SER TYR ARG SER TYR TRP SER          
SEQRES  16 A  287  TRP VAL LEU LEU GLU ILE LEU ARG ASP PHE ARG GLY THR          
SEQRES  17 A  287  LEU SER ILE LYS ASP LEU SER GLN MET THR SER ILE THR          
SEQRES  18 A  287  GLN ASN ASP ILE ILE SER THR LEU GLN SER LEU ASN MET          
SEQRES  19 A  287  VAL LYS TYR TRP LYS GLY GLN HIS VAL ILE CSO VAL THR          
SEQRES  20 A  287  PRO LYS LEU VAL GLU GLU HIS LEU LYS SER ALA GLN TYR          
SEQRES  21 A  287  LYS LYS PRO PRO ILE THR VAL ASP SER VAL CYS LEU LYS          
SEQRES  22 A  287  TRP ALA PRO PRO LYS HIS LYS GLN VAL LYS LEU SER LYS          
SEQRES  23 A  287  LYS                                                          
SEQRES   1 B   74  GLY ALA MET GLY GLU THR SER VAL LEU ALA VAL PRO SER          
SEQRES   2 B   74  TRP ARG ASP HIS SER VAL GLU PRO LEU ARG ASP PRO ASN          
SEQRES   3 B   74  PRO SER ASP ILE LEU GLU ASN LEU ASP ASP SER VAL PHE          
SEQRES   4 B   74  SER LYS ARG HIS ALA LYS LEU GLU LEU ASP GLU LYS ARG          
SEQRES   5 B   74  ARG LYS ARG TRP ASP ILE GLN ARG ILE ARG GLU GLN ARG          
SEQRES   6 B   74  ILE LEU GLN ARG LEU GLN LEU ARG MET                          
MODRES 2Y0M ALY A  274  LYS  N(6)-ACETYLLYSINE                                  
MODRES 2Y0M CSO A  316  CYS  S-HYDROXYCYSTEINE                                  
MODRES 2Y0M CSO A  416  CYS  S-HYDROXYCYSTEINE                                  
HET    ALY  A 274      12                                                       
HET    CSO  A 316       7                                                       
HET    CSO  A 416       7                                                       
HET    ACO  A1450      51                                                       
HET     ZN  A1451       1                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     ACO ACETYL COENZYME *A                                               
HETNAM      ZN ZINC ION                                                         
FORMUL   1  ALY    C8 H16 N2 O3                                                 
FORMUL   2  CSO    2(C3 H7 N O3 S)                                              
FORMUL   3  ACO    C23 H38 N7 O17 P3 S                                          
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  HOH   *10(H2 O)                                                     
HELIX    1   1 PRO A  198  LYS A  203  5                                   6    
HELIX    2   2 TYR A  219  GLY A  228  1                                  10    
HELIX    3   3 HIS A  256  LEU A  269  1                                  14    
HELIX    4   4 PRO A  321  GLN A  324  5                                   4    
HELIX    5   5 GLY A  327  LEU A  342  1                                  16    
HELIX    6   6 SER A  354  PHE A  376  1                                  23    
HELIX    7   7 SER A  381  SER A  390  1                                  10    
HELIX    8   8 THR A  392  LEU A  403  1                                  12    
HELIX    9   9 THR A  418  SER A  428  1                                  11    
HELIX   10  10 ASP A  439  CYS A  442  5                                   4    
HELIX   11  11 ASP B  501  ARG B  535  1                                  35    
SHEET    1  AA 4 TYR A 187  ASP A 190  0                                        
SHEET    2  AA 4 LYS A 181  ILE A 184 -1  O  ILE A 182   N  ILE A 189           
SHEET    3  AA 4 LYS A 206  LEU A 209  1  O  LEU A 207   N  HIS A 183           
SHEET    4  AA 4 TYR A 216  MET A 217 -1  O  MET A 217   N  TRP A 208           
SHEET    1  AB 5 LYS A 238  LYS A 243  0                                        
SHEET    2  AB 5 ILE A 246  ASP A 252 -1  O  ILE A 246   N  LYS A 243           
SHEET    3  AB 5 PHE A 283  VAL A 291 -1  O  PHE A 285   N  VAL A 251           
SHEET    4  AB 5 ALA A 296  GLU A 305 -1  O  HIS A 297   N  GLU A 290           
SHEET    5  AB 5 ILE A 317  THR A 319 -1  O  LEU A 318   N  TYR A 301           
SHEET    1  AC 2 VAL A 406  TRP A 409  0                                        
SHEET    2  AC 2 GLN A 412  ILE A 415 -1  O  GLN A 412   N  TRP A 409           
LINK         C   HIS A 273                 N   ALY A 274     1555   1555  1.33  
LINK         C   ALY A 274                 N   THR A 275     1555   1555  1.33  
LINK         C   ALA A 315                 N   CSO A 316     1555   1555  1.33  
LINK         C   CSO A 316                 N   ILE A 317     1555   1555  1.33  
LINK         C   ILE A 415                 N   CSO A 416     1555   1555  1.33  
LINK         C   CSO A 416                 N   VAL A 417     1555   1555  1.33  
LINK        ZN    ZN A1451                 NE2 HIS A 226     1555   1555  2.07  
LINK        ZN    ZN A1451                 SG  CYS A 230     1555   1555  2.43  
LINK        ZN    ZN A1451                 SG  CYS A 213     1555   1555  2.35  
LINK        ZN    ZN A1451                 SG  CYS A 210     1555   1555  2.25  
CISPEP   1 LYS A  351    PRO A  352          0         2.76                     
SITE     1 AC1 23 TRP A 192  PHE A 270  LEU A 271  ALA A 315                    
SITE     2 AC1 23 CSO A 316  ILE A 317  LEU A 318  THR A 319                    
SITE     3 AC1 23 GLN A 324  ARG A 325  ARG A 326  GLY A 327                    
SITE     4 AC1 23 TYR A 328  GLY A 329  LYS A 330  SER A 354                    
SITE     5 AC1 23 LEU A 356  SER A 360  SER A 363  TYR A 408                    
SITE     6 AC1 23 LYS A 432  HOH A2009  HOH A2010                               
SITE     1 AC2  4 CYS A 210  CYS A 213  HIS A 226  CYS A 230                    
CRYST1  180.940  180.940   80.750  90.00  90.00  90.00 I 41 2 2     16          
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      0.005527  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005527  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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