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Database: PDB
Entry: 4YYK
LinkDB: 4YYK
Original site: 4YYK 
HEADER    PROTEIN BINDING                         24-MAR-15   4YYK              
TITLE     CRYSTAL STRUCTURE OF BRD9 BROMODOMAIN BOUND TO A CROTONYLLYSINE       
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 9;                          
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 17-123);                         
COMPND   5 SYNONYM: RHABDOMYOSARCOMA ANTIGEN MU-RMS-40.8, BRD9;                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE H4;                                                
COMPND   9 CHAIN: C, F;                                                         
COMPND  10 FRAGMENT: N-TERMINAL TAIL (UNP RESIDUES 2-12);                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: LYSINE RESIDUES CROTONYLATED                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRD9, UNQ3040/PRO9856;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRSF;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    BROMODOMAIN-CROTONYLLYSINE COMPLEX, PROTEIN BINDING                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TANG,S.BELLON,A.G.COCHRAN,F.POY                                     
REVDAT   3   14-OCT-15 4YYK    1       JRNL                                     
REVDAT   2   30-SEP-15 4YYK    1       JRNL                                     
REVDAT   1   16-SEP-15 4YYK    0                                                
JRNL        AUTH   E.M.FLYNN,O.W.HUANG,F.POY,M.OPPIKOFER,S.F.BELLON,Y.TANG,     
JRNL        AUTH 2 A.G.COCHRAN                                                  
JRNL        TITL   A SUBSET OF HUMAN BROMODOMAINS RECOGNIZES BUTYRYLLYSINE AND  
JRNL        TITL 2 CROTONYLLYSINE HISTONE PEPTIDE MODIFICATIONS.                
JRNL        REF    STRUCTURE                     V.  23  1801 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26365797                                                     
JRNL        DOI    10.1016/J.STR.2015.08.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 34482                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1851                            
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1928                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3372                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 95                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.52000                                             
REMARK   3    B22 (A**2) : 8.16000                                              
REMARK   3    B33 (A**2) : -6.64000                                             
REMARK   3    B12 (A**2) : -0.84000                                             
REMARK   3    B13 (A**2) : 0.20000                                              
REMARK   3    B23 (A**2) : -2.82000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.036         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.032         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.153         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3458 ; 0.028 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4634 ; 2.846 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   410 ; 7.772 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;37.941 ;23.784       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   624 ;20.322 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;24.631 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   484 ; 0.210 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2584 ; 0.017 ; 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):  1658 ; 3.122 ; 2.457       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2062 ; 3.973 ; 3.667       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1800 ; 3.560 ; 2.601       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.879                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H, H-K, -L                                      
REMARK   3      TWIN FRACTION : 0.121                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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    22        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0322  -0.1050 -34.2189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0155 T22:   0.0100                                     
REMARK   3      T33:   0.0285 T12:  -0.0022                                     
REMARK   3      T13:  -0.0115 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8113 L22:   0.6094                                     
REMARK   3      L33:   0.8678 L12:   0.1610                                     
REMARK   3      L13:   0.4153 L23:  -0.2193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0193 S12:   0.0133 S13:   0.0077                       
REMARK   3      S21:   0.0309 S22:  -0.0345 S23:  -0.0152                       
REMARK   3      S31:   0.0442 S32:  -0.0256 S33:   0.0152                       
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    22        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.1549  23.3179 -66.4459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0421 T22:   0.0048                                     
REMARK   3      T33:   0.0299 T12:   0.0101                                     
REMARK   3      T13:   0.0061 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0343 L22:   0.4710                                     
REMARK   3      L33:   0.4690 L12:   0.0479                                     
REMARK   3      L13:  -0.4183 L23:  -0.2807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:  -0.0026 S13:  -0.0822                       
REMARK   3      S21:  -0.0208 S22:  -0.0081 S23:  -0.0308                       
REMARK   3      S31:  -0.0563 S32:  -0.0020 S33:   0.0135                       
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 :   D    22        D   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3333   0.6140  -1.8211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0065 T22:   0.0076                                     
REMARK   3      T33:   0.0252 T12:   0.0019                                     
REMARK   3      T13:  -0.0012 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7747 L22:   0.7606                                     
REMARK   3      L33:   0.7985 L12:   0.1325                                     
REMARK   3      L13:   0.5267 L23:   0.2407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.0294 S13:   0.0278                       
REMARK   3      S21:  -0.0388 S22:  -0.0076 S23:  -0.0031                       
REMARK   3      S31:   0.0278 S32:  -0.0122 S33:   0.0131                       
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 :   E    22        E   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3435  22.9709  30.3937              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0546 T22:   0.0044                                     
REMARK   3      T33:   0.0383 T12:  -0.0114                                     
REMARK   3      T13:   0.0030 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9763 L22:   0.2354                                     
REMARK   3      L33:   0.7834 L12:  -0.0246                                     
REMARK   3      L13:  -0.7408 L23:   0.2422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0243 S12:   0.0077 S13:  -0.0275                       
REMARK   3      S21:  -0.0179 S22:  -0.0115 S23:   0.0295                       
REMARK   3      S31:  -0.0196 S32:  -0.0082 S33:   0.0357                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4YYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208303.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : DIAMOND(111)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36333                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3HME                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.5, 15% W/V PEG550 MME,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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     GLY A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     ASN A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     ASN B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     LYS B   123                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     SER D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     GLU D    19                                                      
REMARK 465     ASN D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     LYS D   123                                                      
REMARK 465     GLY E    16                                                      
REMARK 465     SER E    17                                                      
REMARK 465     ALA E    18                                                      
REMARK 465     GLU E    19                                                      
REMARK 465     ASN E    20                                                      
REMARK 465     GLU E    21                                                      
REMARK 465     LYS E   123                                                      
REMARK 465     SER F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A  57   CE1   TYR A  57   CZ      0.118                       
REMARK 500    ASP A  66   C     ASP A  66   O       0.117                       
REMARK 500    PHE B  45   C     PHE B  45   O       0.209                       
REMARK 500    GLY E  43   N     GLY E  43   CA      0.105                       
REMARK 500    PHE E  89   CB    PHE E  89   CG      0.105                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  28   CB  -  CG  -  CD1 ANGL. DEV. = -11.6 DEGREES          
REMARK 500    MET A  70   CG  -  SD  -  CE  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ASP A  72   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU A  91   CB  -  CG  -  CD1 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASP B  51   CB  -  CG  -  OD2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    LEU B  91   CB  -  CG  -  CD1 ANGL. DEV. = -13.1 DEGREES          
REMARK 500    ASP B  94   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    LEU D  33   CB  -  CG  -  CD1 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    PRO D  48   C   -  N   -  CA  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LEU D  91   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    MET D  97   CG  -  SD  -  CE  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    LEU E  36   CB  -  CG  -  CD2 ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ASP E  66   CB  -  CG  -  OD2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    PHE E  67   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    PHE E  67   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ASP E  94   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP E  94   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ILE E 113   CG1 -  CB  -  CG2 ANGL. DEV. = -15.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  39       -2.56    -59.71                                   
REMARK 500    ILE A  60      -47.42   -134.49                                   
REMARK 500    ASP A 103        5.38    -63.16                                   
REMARK 500    ASN B  77       59.23     35.85                                   
REMARK 500    PRO B 102      -34.11    -39.91                                   
REMARK 500    ILE D  74      -74.08    -64.33                                   
REMARK 500    VAL D  75      -32.06    -35.29                                   
REMARK 500    ASP E  40       61.46   -108.09                                   
REMARK 500    PHE E  44      -36.40    -33.88                                   
REMARK 500    PRO E  55      112.90    -34.39                                   
REMARK 500    ALA E  76       33.47    -79.00                                   
REMARK 500    ASN E  77       54.01     12.79                                   
REMARK 500    ARG E 101      132.35    -38.64                                   
REMARK 500    ASP E 103        8.35    -66.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE D  32        -11.54                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YY4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YY6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YYN   RELATED DB: PDB                                   
DBREF  4YYK A   17   123  UNP    Q9H8M2   BRD9_HUMAN      17    123             
DBREF  4YYK B   17   123  UNP    Q9H8M2   BRD9_HUMAN      17    123             
DBREF  4YYK C    1    11  UNP    P62805   H4_HUMAN         2     12             
DBREF  4YYK D   17   123  UNP    Q9H8M2   BRD9_HUMAN      17    123             
DBREF  4YYK E   17   123  UNP    Q9H8M2   BRD9_HUMAN      17    123             
DBREF  4YYK F    1    11  UNP    P62805   H4_HUMAN         2     12             
SEQADV 4YYK GLY A   16  UNP  Q9H8M2              EXPRESSION TAG                 
SEQADV 4YYK GLY B   16  UNP  Q9H8M2              EXPRESSION TAG                 
SEQADV 4YYK GLY D   16  UNP  Q9H8M2              EXPRESSION TAG                 
SEQADV 4YYK GLY E   16  UNP  Q9H8M2              EXPRESSION TAG                 
SEQRES   1 A  108  GLY SER ALA GLU ASN GLU SER THR PRO ILE GLN GLN LEU          
SEQRES   2 A  108  LEU GLU HIS PHE LEU ARG GLN LEU GLN ARG LYS ASP PRO          
SEQRES   3 A  108  HIS GLY PHE PHE ALA PHE PRO VAL THR ASP ALA ILE ALA          
SEQRES   4 A  108  PRO GLY TYR SER MET ILE ILE LYS HIS PRO MET ASP PHE          
SEQRES   5 A  108  GLY THR MET LYS ASP LYS ILE VAL ALA ASN GLU TYR LYS          
SEQRES   6 A  108  SER VAL THR GLU PHE LYS ALA ASP PHE LYS LEU MET CYS          
SEQRES   7 A  108  ASP ASN ALA MET THR TYR ASN ARG PRO ASP THR VAL TYR          
SEQRES   8 A  108  TYR LYS LEU ALA LYS LYS ILE LEU HIS ALA GLY PHE LYS          
SEQRES   9 A  108  MET MET SER LYS                                              
SEQRES   1 B  108  GLY SER ALA GLU ASN GLU SER THR PRO ILE GLN GLN LEU          
SEQRES   2 B  108  LEU GLU HIS PHE LEU ARG GLN LEU GLN ARG LYS ASP PRO          
SEQRES   3 B  108  HIS GLY PHE PHE ALA PHE PRO VAL THR ASP ALA ILE ALA          
SEQRES   4 B  108  PRO GLY TYR SER MET ILE ILE LYS HIS PRO MET ASP PHE          
SEQRES   5 B  108  GLY THR MET LYS ASP LYS ILE VAL ALA ASN GLU TYR LYS          
SEQRES   6 B  108  SER VAL THR GLU PHE LYS ALA ASP PHE LYS LEU MET CYS          
SEQRES   7 B  108  ASP ASN ALA MET THR TYR ASN ARG PRO ASP THR VAL TYR          
SEQRES   8 B  108  TYR LYS LEU ALA LYS LYS ILE LEU HIS ALA GLY PHE LYS          
SEQRES   9 B  108  MET MET SER LYS                                              
SEQRES   1 C   11  SER GLY ARG GLY KCR GLY GLY KCR GLY LEU GLY                  
SEQRES   1 D  108  GLY SER ALA GLU ASN GLU SER THR PRO ILE GLN GLN LEU          
SEQRES   2 D  108  LEU GLU HIS PHE LEU ARG GLN LEU GLN ARG LYS ASP PRO          
SEQRES   3 D  108  HIS GLY PHE PHE ALA PHE PRO VAL THR ASP ALA ILE ALA          
SEQRES   4 D  108  PRO GLY TYR SER MET ILE ILE LYS HIS PRO MET ASP PHE          
SEQRES   5 D  108  GLY THR MET LYS ASP LYS ILE VAL ALA ASN GLU TYR LYS          
SEQRES   6 D  108  SER VAL THR GLU PHE LYS ALA ASP PHE LYS LEU MET CYS          
SEQRES   7 D  108  ASP ASN ALA MET THR TYR ASN ARG PRO ASP THR VAL TYR          
SEQRES   8 D  108  TYR LYS LEU ALA LYS LYS ILE LEU HIS ALA GLY PHE LYS          
SEQRES   9 D  108  MET MET SER LYS                                              
SEQRES   1 E  108  GLY SER ALA GLU ASN GLU SER THR PRO ILE GLN GLN LEU          
SEQRES   2 E  108  LEU GLU HIS PHE LEU ARG GLN LEU GLN ARG LYS ASP PRO          
SEQRES   3 E  108  HIS GLY PHE PHE ALA PHE PRO VAL THR ASP ALA ILE ALA          
SEQRES   4 E  108  PRO GLY TYR SER MET ILE ILE LYS HIS PRO MET ASP PHE          
SEQRES   5 E  108  GLY THR MET LYS ASP LYS ILE VAL ALA ASN GLU TYR LYS          
SEQRES   6 E  108  SER VAL THR GLU PHE LYS ALA ASP PHE LYS LEU MET CYS          
SEQRES   7 E  108  ASP ASN ALA MET THR TYR ASN ARG PRO ASP THR VAL TYR          
SEQRES   8 E  108  TYR LYS LEU ALA LYS LYS ILE LEU HIS ALA GLY PHE LYS          
SEQRES   9 E  108  MET MET SER LYS                                              
SEQRES   1 F   11  SER GLY ARG GLY KCR GLY GLY KCR GLY LEU GLY                  
MODRES 4YYK KCR C    5  LYS  MODIFIED RESIDUE                                   
MODRES 4YYK KCR C    8  LYS  MODIFIED RESIDUE                                   
MODRES 4YYK KCR F    5  LYS  MODIFIED RESIDUE                                   
MODRES 4YYK KCR F    8  LYS  MODIFIED RESIDUE                                   
HET    KCR  C   5      14                                                       
HET    KCR  C   8      14                                                       
HET    KCR  F   5      14                                                       
HET    KCR  F   8      14                                                       
HETNAM     KCR N-6-CROTONYL-L-LYSINE                                            
FORMUL   3  KCR    4(C10 H18 N2 O3)                                             
FORMUL   7  HOH   *95(H2 O)                                                     
HELIX    1 AA1 THR A   23  LYS A   39  1                                  17    
HELIX    2 AA2 GLY A   56  ILE A   60  5                                   5    
HELIX    3 AA3 ASP A   66  ASN A   77  1                                  12    
HELIX    4 AA4 SER A   81  ASN A  100  1                                  20    
HELIX    5 AA5 THR A  104  MET A  121  1                                  18    
HELIX    6 AA6 THR B   23  ARG B   38  1                                  16    
HELIX    7 AA7 GLY B   56  ILE B   61  1                                   6    
HELIX    8 AA8 ASP B   66  ALA B   76  1                                  11    
HELIX    9 AA9 SER B   81  ASN B  100  1                                  20    
HELIX   10 AB1 THR B  104  MET B  121  1                                  18    
HELIX   11 AB2 THR D   23  ARG D   38  1                                  16    
HELIX   12 AB3 ASP D   66  ALA D   76  1                                  11    
HELIX   13 AB4 SER D   81  ASN D  100  1                                  20    
HELIX   14 AB5 THR D  104  MET D  121  1                                  18    
HELIX   15 AB6 THR E   23  LYS E   39  1                                  17    
HELIX   16 AB7 GLY E   56  ILE E   60  5                                   5    
HELIX   17 AB8 ASP E   66  ALA E   76  1                                  11    
HELIX   18 AB9 SER E   81  ASN E  100  1                                  20    
HELIX   19 AC1 THR E  104  MET E  121  1                                  18    
LINK         C   GLY C   4                 N   KCR C   5     1555   1555  1.35  
LINK         C   KCR C   5                 N   GLY C   6     1555   1555  1.36  
LINK         C   GLY C   7                 N   KCR C   8     1555   1555  1.34  
LINK         C   KCR C   8                 N   GLY C   9     1555   1555  1.34  
LINK         C   GLY F   4                 N   KCR F   5     1555   1555  1.34  
LINK         C   KCR F   5                 N   GLY F   6     1555   1555  1.35  
LINK         C   GLY F   7                 N   KCR F   8     1555   1555  1.34  
LINK         C   KCR F   8                 N   GLY F   9     1555   1555  1.33  
CRYST1   24.840   34.730  129.080  89.88  89.81  69.45 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.040258 -0.015092 -0.000119        0.00000                         
SCALE2      0.000000  0.030750 -0.000031        0.00000                         
SCALE3      0.000000  0.000000  0.007747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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