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Database: PDB
Entry: 5MYG
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Original site: 5MYG 
HEADER    TRANSCRIPTION                           26-JAN-17   5MYG              
TITLE     CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRPF1 IN COMPLEX WITH   
TITLE    2 NI-57 CHEMICAL PROBE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1,PROTEIN     
COMPND   5 BR140;                                                               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRPF1, BR140;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TRANSCRIPTION, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,   
KEYWDS   2 SGC                                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TALLANT,N.IGOE,E.D.BAYLE,T.KROJER,G.NUNEZ-ALONSO,J.KOPEC,           
AUTHOR   2 F.FITZPATRICK,P.SAVITSKY,O.FEDOROV,P.E.BRENNAN,F.VON DELFT,          
AUTHOR   3 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.MULLER,P.FISH,S.KNAPP,        
AUTHOR   4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   2   06-SEP-17 5MYG    1       JRNL                                     
REVDAT   1   09-AUG-17 5MYG    0                                                
JRNL        AUTH   N.IGOE,E.D.BAYLE,C.TALLANT,O.FEDOROV,J.C.MEIER,P.SAVITSKY,   
JRNL        AUTH 2 C.ROGERS,Y.MORIAS,S.SCHOLZE,H.BOYD,D.CUNOOSAMY,D.M.ANDREWS,  
JRNL        AUTH 3 A.CHEASTY,P.E.BRENNAN,S.MULLER,S.KNAPP,P.V.FISH              
JRNL        TITL   DESIGN OF A CHEMICAL PROBE FOR THE BROMODOMAIN AND PLANT     
JRNL        TITL 2 HOMEODOMAIN FINGER-CONTAINING (BRPF) FAMILY OF PROTEINS.     
JRNL        REF    J. MED. CHEM.                 V.  60  6998 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28714688                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00611                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1682                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 28659                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.307                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1445                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.8795 -  4.9456    1.00     2966   145  0.1743 0.1997        
REMARK   3     2  4.9456 -  3.9286    0.98     2765   137  0.1960 0.2543        
REMARK   3     3  3.9286 -  3.4329    0.90     2490   129  0.3049 0.4021        
REMARK   3     4  3.4329 -  3.1194    1.00     2747   149  0.2596 0.3210        
REMARK   3     5  3.1194 -  2.8961    1.00     2739   143  0.2753 0.3164        
REMARK   3     6  2.8961 -  2.7255    1.00     2749   138  0.2677 0.3323        
REMARK   3     7  2.7255 -  2.5891    1.00     2711   157  0.2672 0.3394        
REMARK   3     8  2.5891 -  2.4764    1.00     2652   152  0.2645 0.3269        
REMARK   3     9  2.4764 -  2.3811    1.00     2755   144  0.2786 0.3640        
REMARK   3    10  2.3811 -  2.2990    0.99     2640   151  0.3009 0.3421        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.55                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           3937                                  
REMARK   3   ANGLE     :  1.344           5322                                  
REMARK   3   CHIRALITY :  0.060            558                                  
REMARK   3   PLANARITY :  0.007            798                                  
REMARK   3   DIHEDRAL  : 14.277           1572                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 626:740)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8232  12.7820 -22.4843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2990 T22:   0.2045                                     
REMARK   3      T33:   0.2778 T12:   0.0766                                     
REMARK   3      T13:  -0.0657 T23:  -0.0588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9673 L22:   2.0580                                     
REMARK   3      L33:   2.2420 L12:   1.3596                                     
REMARK   3      L13:  -0.6466 L23:  -1.3974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1365 S12:  -0.1829 S13:  -0.1153                       
REMARK   3      S21:  -0.0244 S22:  -0.3022 S23:   0.0911                       
REMARK   3      S31:  -0.1525 S32:   0.2942 S33:   0.1471                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 626:740)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3159 -13.2409 -41.4512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3188 T22:   0.2565                                     
REMARK   3      T33:   0.2916 T12:   0.1010                                     
REMARK   3      T13:   0.0290 T23:  -0.0877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2544 L22:   0.9254                                     
REMARK   3      L33:   3.8016 L12:   0.6918                                     
REMARK   3      L13:   0.3825 L23:   0.4152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0311 S12:   0.2788 S13:   0.2491                       
REMARK   3      S21:  -0.1766 S22:  -0.0821 S23:   0.1934                       
REMARK   3      S31:  -0.0984 S32:   0.0043 S33:   0.0214                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 629:740)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2296  24.6558  -3.4146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2761 T22:   0.4049                                     
REMARK   3      T33:   0.2611 T12:  -0.0527                                     
REMARK   3      T13:   0.0213 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1862 L22:   2.2357                                     
REMARK   3      L33:   3.5735 L12:   1.3142                                     
REMARK   3      L13:  -1.1045 L23:  -1.0874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0965 S12:  -0.1094 S13:   0.1048                       
REMARK   3      S21:   0.0174 S22:  -0.1522 S23:   0.1232                       
REMARK   3      S31:  -0.0975 S32:   0.1226 S33:   0.0583                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 630:740)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6211 -24.6615 -22.4450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2772 T22:   0.3138                                     
REMARK   3      T33:   0.2596 T12:   0.0178                                     
REMARK   3      T13:  -0.0198 T23:  -0.1208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3167 L22:   2.2813                                     
REMARK   3      L33:   2.3691 L12:   1.5344                                     
REMARK   3      L13:   0.9221 L23:  -0.0593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1434 S12:  -0.2102 S13:   0.1339                       
REMARK   3      S21:   0.0416 S22:  -0.0109 S23:   0.0807                       
REMARK   3      S31:   0.2926 S32:   0.0715 S33:  -0.0973                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003232.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5 - 7.5                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28990                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.880                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: 4LC2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 17% PEG 10K,     
REMARK 280  0.1 M BIS-TRIS PH 5.5, PH 7.5, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.85800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.53650            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.85800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       68.53650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   625                                                      
REMARK 465     SER B   625                                                      
REMARK 465     SER C   625                                                      
REMARK 465     MET C   626                                                      
REMARK 465     GLU C   627                                                      
REMARK 465     MET C   628                                                      
REMARK 465     SER D   625                                                      
REMARK 465     MET D   626                                                      
REMARK 465     GLU D   627                                                      
REMARK 465     MET D   628                                                      
REMARK 465     GLN D   629                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 670    CD   CE   NZ                                        
REMARK 470     LYS A 738    CE   NZ                                             
REMARK 470     LYS B 670    CD   CE   NZ                                        
REMARK 470     LYS B 738    CE   NZ                                             
REMARK 470     LYS C 670    CD   CE   NZ                                        
REMARK 470     LYS C 671    NZ                                                  
REMARK 470     ASP D 667    CG   OD1  OD2                                       
REMARK 470     LYS D 670    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C   655     NE2  GLN D   680     2555     2.00            
REMARK 500   NE2  GLN C   680     OE1  GLU D   655     2555     2.07            
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    ASP D 711       52.11   -115.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LS8 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LS8 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LS8 C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LS8 D 801                 
DBREF  5MYG A  626   740  UNP    P55201   BRPF1_HUMAN    626    740             
DBREF  5MYG B  626   740  UNP    P55201   BRPF1_HUMAN    626    740             
DBREF  5MYG C  626   740  UNP    P55201   BRPF1_HUMAN    626    740             
DBREF  5MYG D  626   740  UNP    P55201   BRPF1_HUMAN    626    740             
SEQADV 5MYG SER A  625  UNP  P55201              EXPRESSION TAG                 
SEQADV 5MYG SER B  625  UNP  P55201              EXPRESSION TAG                 
SEQADV 5MYG SER C  625  UNP  P55201              EXPRESSION TAG                 
SEQADV 5MYG SER D  625  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  116  SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU          
SEQRES   2 A  116  ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY          
SEQRES   3 A  116  ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO          
SEQRES   4 A  116  ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE          
SEQRES   5 A  116  THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN          
SEQRES   6 A  116  PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER          
SEQRES   7 A  116  ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR          
SEQRES   8 A  116  ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL          
SEQRES   9 A  116  LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY              
SEQRES   1 B  116  SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU          
SEQRES   2 B  116  ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY          
SEQRES   3 B  116  ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO          
SEQRES   4 B  116  ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE          
SEQRES   5 B  116  THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN          
SEQRES   6 B  116  PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER          
SEQRES   7 B  116  ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR          
SEQRES   8 B  116  ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL          
SEQRES   9 B  116  LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY              
SEQRES   1 C  116  SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU          
SEQRES   2 C  116  ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY          
SEQRES   3 C  116  ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO          
SEQRES   4 C  116  ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE          
SEQRES   5 C  116  THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN          
SEQRES   6 C  116  PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER          
SEQRES   7 C  116  ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR          
SEQRES   8 C  116  ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL          
SEQRES   9 C  116  LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY              
SEQRES   1 D  116  SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU          
SEQRES   2 D  116  ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY          
SEQRES   3 D  116  ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO          
SEQRES   4 D  116  ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE          
SEQRES   5 D  116  THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN          
SEQRES   6 D  116  PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER          
SEQRES   7 D  116  ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR          
SEQRES   8 D  116  ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL          
SEQRES   9 D  116  LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY              
HET    LS8  A 801      27                                                       
HET    LS8  B 801      27                                                       
HET    LS8  C 801      27                                                       
HET    LS8  D 801      27                                                       
HETNAM     LS8 4-CYANO-~{N}-(1,3-DIMETHYL-2-OXIDANYLIDENE-QUINOLIN-6-           
HETNAM   2 LS8  YL)-2-METHOXY-BENZENESULFONAMIDE                                
FORMUL   5  LS8    4(C19 H17 N3 O4 S)                                           
FORMUL   9  HOH   *76(H2 O)                                                     
HELIX    1 AA1 GLN A  629  ASP A  648  1                                  20    
HELIX    2 AA2 ASP A  674  ALA A  684  1                                  11    
HELIX    3 AA3 ASN A  689  ASN A  708  1                                  20    
HELIX    4 AA4 THR A  712  GLU A  737  1                                  26    
HELIX    5 AA5 GLN B  629  ASP B  648  1                                  20    
HELIX    6 AA6 ASP B  664  ILE B  669  1                                   6    
HELIX    7 AA7 ASP B  674  ALA B  684  1                                  11    
HELIX    8 AA8 ASN B  689  ASN B  708  1                                  20    
HELIX    9 AA9 THR B  712  LYS B  738  1                                  27    
HELIX   10 AB1 THR C  631  ASP C  648  1                                  18    
HELIX   11 AB2 ASP C  664  ILE C  669  1                                   6    
HELIX   12 AB3 ASP C  674  ALA C  684  1                                  11    
HELIX   13 AB4 ASN C  689  ASN C  708  1                                  20    
HELIX   14 AB5 THR C  712  LYS C  738  1                                  27    
HELIX   15 AB6 THR D  631  ASP D  648  1                                  18    
HELIX   16 AB7 ASP D  664  ILE D  669  1                                   6    
HELIX   17 AB8 ASP D  674  ALA D  684  1                                  11    
HELIX   18 AB9 ASN D  689  ASN D  708  1                                  20    
HELIX   19 AC1 THR D  712  LYS D  738  1                                  27    
SITE     1 AC1 10 ASN A 651  ILE A 652  PHE A 653  PRO A 658                    
SITE     2 AC1 10 TYR A 707  ASN A 708  PHE A 714  HOH A 908                    
SITE     3 AC1 10 ASP B 711  ARG B 716                                          
SITE     1 AC2  8 ILE B 652  PHE B 653  VAL B 657  PRO B 658                    
SITE     2 AC2  8 GLU B 661  TYR B 707  ASN B 708  PHE B 714                    
SITE     1 AC3 10 ILE C 652  PHE C 653  PRO C 658  GLU C 661                    
SITE     2 AC3 10 VAL C 662  TYR C 707  ASN C 708  PHE C 714                    
SITE     3 AC3 10 HOH C 907  ARG D 686                                          
SITE     1 AC4 11 ILE C 713  ASN D 651  ILE D 652  VAL D 657                    
SITE     2 AC4 11 PRO D 658  GLU D 661  VAL D 662  TYR D 707                    
SITE     3 AC4 11 ASN D 708  PHE D 714  HOH D 907                               
CRYST1   37.140  123.716  137.073  90.00  90.00  90.00 P 2 21 21    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      0.026925  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008083  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007295        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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