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Database: PDB
Entry: 5LVQ
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Original site: 5LVQ 
HEADER    TRANSFERASE                             14-SEP-16   5LVQ              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCAF BROMODOMAIN IN COMPLEX WITH COMPOUND-D
TITLE    2 (CPD-D), N-METHYL-2-(TETRAHYDRO-2H-PYRAN-4-YLOXY)BENZAMIDE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT2B;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HISTONE ACETYLTRANSFERASE PCAF,HISTONE ACETYLASE PCAF,LYSINE
COMPND   5 ACETYLTRANSFERASE 2B,P300/CBP-ASSOCIATED FACTOR,P/CAF;               
COMPND   6 EC: 2.3.1.48;                                                        
COMPND   7 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: KAT2B, PCAF;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    SIGNALING PROTEIN, BROMODOMAIN, HISTONE ACETYLTRANSFERASE KAT2B,      
KEYWDS   2 HISTONE, ACETYLATION, ACETYLLYSINE, EPIGENETICS, STRUCTURAL GENOMICS 
KEYWDS   3 CONSORTIUM (SGC), TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,P.FILIPPAKOPOULOS,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,    
AUTHOR   2 A.M.EDWARDS,A.L.HOPKINS,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC) 
REVDAT   2   11-JAN-17 5LVQ    1       JRNL                                     
REVDAT   1   26-OCT-16 5LVQ    0                                                
JRNL        AUTH   I.NAVRATILOVA,T.ARISTOTELOUS,S.PICAUD,A.CHAIKUAD,S.KNAPP,    
JRNL        AUTH 2 P.FILAPPAKOPOULOS,A.L.HOPKINS                                
JRNL        TITL   DISCOVERY OF NEW BROMODOMAIN SCAFFOLDS BY BIOSENSOR FRAGMENT 
JRNL        TITL 2 SCREENING.                                                   
JRNL        REF    ACS MED CHEM LETT             V.   7  1213 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   27994766                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00154                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22306                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1212                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1652                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1792                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.543         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1903 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1808 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2556 ; 1.712 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4184 ; 1.202 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   222 ; 5.812 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;37.930 ;23.778       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   347 ;15.344 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;22.177 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   260 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2124 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   447 ; 0.006 ; 0.020       
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):   871 ; 3.778 ; 4.210       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   872 ; 3.776 ; 4.212       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1087 ; 5.316 ; 6.273       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1088 ; 5.315 ; 6.276       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1032 ; 4.866 ; 4.746       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1033 ; 4.864 ; 4.747       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1466 ; 7.155 ; 6.894       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2345 ; 9.815 ;34.973       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2346 ; 9.814 ;34.986       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   724    829       B   724    829    5972  0.14  0.05     
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   724        A   831                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7319  12.8299  53.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1211 T22:   0.1893                                     
REMARK   3      T33:   0.0418 T12:  -0.0479                                     
REMARK   3      T13:  -0.0021 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1546 L22:   3.6544                                     
REMARK   3      L33:   1.3702 L12:  -0.1597                                     
REMARK   3      L13:   1.6899 L23:   0.7166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3694 S12:   0.0967 S13:   0.1243                       
REMARK   3      S21:   0.2705 S22:  -0.5127 S23:   0.0412                       
REMARK   3      S31:   0.1513 S32:  -0.1036 S33:   0.1433                       
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   723        B   830                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5980  17.2460  72.2592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0802 T22:   0.0532                                     
REMARK   3      T33:   0.1391 T12:  -0.0258                                     
REMARK   3      T13:  -0.0144 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8994 L22:   3.5523                                     
REMARK   3      L33:   2.9668 L12:   0.1043                                     
REMARK   3      L13:  -0.5208 L23:   0.8941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0696 S12:   0.3222 S13:  -0.0722                       
REMARK   3      S21:   0.2539 S22:  -0.0348 S23:   0.4934                       
REMARK   3      S31:  -0.0691 S32:   0.0525 S33:  -0.0348                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001447.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 0.91997                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-35% PEG 3350, 0.1 M BIS-TRIS PH 5.5   
REMARK 280  -7.0 OR 21-40% MEDIUM-MOLECULAR-WEIGHT PEG SMEARS (MMW PEG          
REMARK 280  SMEARS) BUFFERED EITHER WITH 0.1 M BIS-TRIS PH 6.0-7.5 OR 0.1 M     
REMARK 280  TRIS PH 7.5-8.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE         
REMARK 280  277.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.92950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.82681            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.58733            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       49.92950            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       28.82681            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.58733            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       49.92950            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       28.82681            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.58733            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.65362            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       67.17467            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       57.65362            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       67.17467            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       57.65362            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       67.17467            
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: MONOMERIC                         
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 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 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   713                                                      
REMARK 465     MET A   714                                                      
REMARK 465     GLY A   715                                                      
REMARK 465     LYS A   716                                                      
REMARK 465     GLU A   717                                                      
REMARK 465     LYS A   718                                                      
REMARK 465     SER A   719                                                      
REMARK 465     LYS A   720                                                      
REMARK 465     GLU A   721                                                      
REMARK 465     PRO A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     SER B   713                                                      
REMARK 465     MET B   714                                                      
REMARK 465     GLY B   715                                                      
REMARK 465     LYS B   716                                                      
REMARK 465     GLU B   717                                                      
REMARK 465     LYS B   718                                                      
REMARK 465     SER B   719                                                      
REMARK 465     LYS B   720                                                      
REMARK 465     GLU B   721                                                      
REMARK 465     PRO B   722                                                      
REMARK 465     ASP B   831                                                      
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     ASP A 724    CG   OD1  OD2                                       
REMARK 470     LYS A 785    CG   CD   CE   NZ                                   
REMARK 470     LEU A 829    CG   CD1  CD2                                       
REMARK 470     ILE A 830    CG1  CG2  CD1                                       
REMARK 470     ASP A 831    CG   OD1  OD2                                       
REMARK 470     ARG B 723    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 830    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL B   752     OH   TYR B   761              2.17            
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 A 726       33.38    -96.31                                   
REMARK 500    ALA B 757       69.03   -156.15                                   
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 EDO A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2LX A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 903                 
DBREF  5LVQ A  715   831  UNP    Q92831   KAT2B_HUMAN    715    831             
DBREF  5LVQ B  715   831  UNP    Q92831   KAT2B_HUMAN    715    831             
SEQADV 5LVQ SER A  713  UNP  Q92831              EXPRESSION TAG                 
SEQADV 5LVQ MET A  714  UNP  Q92831              EXPRESSION TAG                 
SEQADV 5LVQ SER B  713  UNP  Q92831              EXPRESSION TAG                 
SEQADV 5LVQ MET B  714  UNP  Q92831              EXPRESSION TAG                 
SEQRES   1 A  119  SER MET GLY LYS GLU LYS SER LYS GLU PRO ARG ASP PRO          
SEQRES   2 A  119  ASP GLN LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN          
SEQRES   3 A  119  VAL LYS SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO          
SEQRES   4 A  119  VAL LYS ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE          
SEQRES   5 A  119  ARG PHE PRO MET ASP LEU LYS THR MET SER GLU ARG LEU          
SEQRES   6 A  119  LYS ASN ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA          
SEQRES   7 A  119  ASP LEU GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN          
SEQRES   8 A  119  PRO PRO GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU          
SEQRES   9 A  119  GLU LYS PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU          
SEQRES  10 A  119  ILE ASP                                                      
SEQRES   1 B  119  SER MET GLY LYS GLU LYS SER LYS GLU PRO ARG ASP PRO          
SEQRES   2 B  119  ASP GLN LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN          
SEQRES   3 B  119  VAL LYS SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO          
SEQRES   4 B  119  VAL LYS ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE          
SEQRES   5 B  119  ARG PHE PRO MET ASP LEU LYS THR MET SER GLU ARG LEU          
SEQRES   6 B  119  LYS ASN ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA          
SEQRES   7 B  119  ASP LEU GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN          
SEQRES   8 B  119  PRO PRO GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU          
SEQRES   9 B  119  GLU LYS PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU          
SEQRES  10 B  119  ILE ASP                                                      
HET    EDO  A 901       4                                                       
HET    EDO  A 902       4                                                       
HET    EDO  A 903       4                                                       
HET    2LX  A 904      17                                                       
HET    EDO  B 901       4                                                       
HET    EDO  B 902       4                                                       
HET    DMS  B 903       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     2LX N-METHYL-2-(TETRAHYDRO-2H-PYRAN-4-YLOXY)BENZAMIDE                
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    5(C2 H6 O2)                                                  
FORMUL   6  2LX    C13 H17 N O3                                                 
FORMUL   9  DMS    C2 H6 O S                                                    
FORMUL  10  HOH   *127(H2 O)                                                    
HELIX    1 AA1 ASP A  726  HIS A  742  1                                  17    
HELIX    2 AA2 ALA A  745  MET A  749  5                                   5    
HELIX    3 AA3 GLY A  759  ILE A  764  1                                   6    
HELIX    4 AA4 ASP A  769  ASN A  779  1                                  11    
HELIX    5 AA5 SER A  784  ASN A  803  1                                  20    
HELIX    6 AA6 SER A  807  ALA A  827  1                                  21    
HELIX    7 AA7 ASP B  724  HIS B  742  1                                  19    
HELIX    8 AA8 ALA B  745  MET B  749  5                                   5    
HELIX    9 AA9 GLY B  759  ILE B  764  1                                   6    
HELIX   10 AB1 ASP B  769  ASN B  779  1                                  11    
HELIX   11 AB2 SER B  784  ASN B  803  1                                  20    
HELIX   12 AB3 SER B  807  ALA B  827  1                                  21    
SITE     1 AC1  5 ARG A 776  ASN A 779  TYR A 781  GLU B 775                    
SITE     2 AC1  5 ASN B 779                                                     
SITE     1 AC2  2 GLY A 828  ILE A 830                                          
SITE     1 AC3  4 LYS A 733  GLN A 737  SER A 774  HOH A1005                    
SITE     1 AC4  8 PRO A 747  PHE A 748  GLU A 756  ALA A 757                    
SITE     2 AC4  8 ASN A 803  HOH A1002  HOH A1040  HOH B1026                    
SITE     1 AC5  4 GLN B 737  LYS B 740  SER B 774  LYS B 778                    
SITE     1 AC6  5 PRO B 747  THR B 755  TYR B 809  DMS B 903                    
SITE     2 AC6  5 HOH B1003                                                     
SITE     1 AC7  4 PRO B 747  ASN B 803  EDO B 902  HOH B1004                    
CRYST1   99.859   99.859  100.762  90.00  90.00 120.00 H 3          18          
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      0.010014  0.005782  0.000000        0.00000                         
SCALE2      0.000000  0.011563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009924        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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