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Database: PDB
Entry: 2OU2
LinkDB: 2OU2
Original site: 2OU2 
HEADER    TRANSFERASE                             09-FEB-07   2OU2              
TITLE     ACETYLTRANSFERASE DOMAIN OF HUMAN HIV-1 TAT INTERACTING               
TITLE    2 PROTEIN, 60KDA, ISOFORM 3                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE ACETYLTRANSFERASE HTATIP;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ACETYLTRANSFERASE DOMAIN;                                  
COMPND   5 SYNONYM: 60 KDA TAT INTERACTIVE PROTEIN, TIP60, HIV-1 TAT            
COMPND   6 INTERACTIVE PROTEIN, CPLA(2)-INTERACTING PROTEIN;                    
COMPND   7 EC: 2.3.1.48;                                                        
COMPND   8 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: HTATIP, TIP60;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A_MHL                                
KEYWDS    HISTONE ACETYLTRANSFERASE HTATIP, TIP, TIP60, STRUCTURAL              
KEYWDS   2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MIN,H.WU,L.DOMBROVSKI,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,              
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,                
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   2   24-FEB-09 2OU2    1       VERSN                                    
REVDAT   1   27-FEB-07 2OU2    0                                                
JRNL        AUTH   H.WU,J.MIN,L.DOMBROVSKI,P.LOPPNAU,J.WEIGELT,                 
JRNL        AUTH 2 M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,          
JRNL        AUTH 3 A.N.PLOTNIKOV                                                
JRNL        TITL   THE CRYSTAL STRUCTURE OF ACETYLTRANSFERASE DOMAIN            
JRNL        TITL 2 OF HUMAN HIV-1 TAT INTERACTING PROTEIN IN COMPLEX            
JRNL        TITL 3 WITH ACETYLCOENZYME A.                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16701                          
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 893                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1210                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2046                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 30                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.99000                                              
REMARK   3    B22 (A**2) : 0.99000                                              
REMARK   3    B33 (A**2) : -1.99000                                             
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): 0.263         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.151         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.075         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2150 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2908 ; 1.455 ; 2.014       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   243 ; 6.716 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;32.377 ;23.474       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   385 ;16.361 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;19.835 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   314 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1575 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   862 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1437 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    75 ; 0.157 ; 0.200       
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):    28 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.177 ; 0.200       
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):  1272 ; 0.829 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1998 ; 1.418 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1025 ; 1.973 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   910 ; 3.055 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2OU2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041585.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17598                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2GIV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED HTATIP WAS COMPLEXED WITH       
REMARK 280  ACETYLCOENZYME A (ACCOA) (SIGMA) AT 1:10 MOLAR RATIO OF             
REMARK 280  PROTEIN:ACCOA AND CRYSTALLIZED USING THE HANGING DROP VAPOR         
REMARK 280  DIFFUSION METHOD AT 20 DEG C BY MIXING 1 MICROLITER OF THE          
REMARK 280  PROTEIN SOLUTION WITH 1 MICROLITER OF THE RESERVOIR SOLUTION        
REMARK 280  CONTAINING 16% PEG3350, 0.2 M AMMONIUM ACETATE, 0.1 M BIS-          
REMARK 280  TRIS, PH 6.6., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       53.81600            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       66.86550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       53.81600            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       66.86550            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       53.81600            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       66.86550            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       53.81600            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       66.86550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       53.81600            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       66.86550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       53.81600            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       66.86550            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       53.81600            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       66.86550            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       53.81600            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       53.81600            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       66.86550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     THR A   175                                                      
REMARK 465     ARG A   176                                                      
REMARK 465     MET A   177                                                      
REMARK 465     MET A   375                                                      
REMARK 465     GLY A   376                                                      
REMARK 465     LEU A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     SER A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     GLU A   383                                                      
REMARK 465     ARG A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     THR A   423                                                      
REMARK 465     LEU A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     ASP A   427                                                      
REMARK 465     ILE A   428                                                      
REMARK 465     VAL A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     ARG A   434                                                      
REMARK 465     ALA A   435                                                      
REMARK 465     MET A   436                                                      
REMARK 465     LEU A   437                                                      
REMARK 465     LYS A   438                                                      
REMARK 465     ARG A   439                                                      
REMARK 465     LEU A   440                                                      
REMARK 465     LYS A   453                                                      
REMARK 465     ASP A   454                                                      
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    LEU A 233      -88.39    -17.46                                   
REMARK 500    PRO A 237     -154.31    -67.16                                   
REMARK 500    ALA A 316      -62.28    -97.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 490  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 214   SG                                                     
REMARK 620 2 HIS A 227   NE2  98.1                                              
REMARK 620 3 CYS A 231   SG  121.5 109.0                                        
REMARK 620 4 CYS A 211   SG  114.3 104.0 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 490                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACO A 500                 
DBREF  2OU2 A  175   454  UNP    Q92993   TIP60_HUMAN    227    506             
SEQADV 2OU2 ALY A  275  UNP  Q92993    LYS   327 MODIFIED RESIDUE               
SEQRES   1 A  280  THR ARG MET LYS ASN ILE GLU CYS ILE GLU LEU GLY ARG          
SEQRES   2 A  280  HIS ARG LEU LYS PRO TRP TYR PHE SER PRO TYR PRO GLN          
SEQRES   3 A  280  GLU LEU THR THR LEU PRO VAL LEU TYR LEU CYS GLU PHE          
SEQRES   4 A  280  CYS LEU LYS TYR GLY ARG SER LEU LYS CYS LEU GLN ARG          
SEQRES   5 A  280  HIS LEU THR LYS CYS ASP LEU ARG HIS PRO PRO GLY ASN          
SEQRES   6 A  280  GLU ILE TYR ARG LYS GLY THR ILE SER PHE PHE GLU ILE          
SEQRES   7 A  280  ASP GLY ARG LYS ASN LYS SER TYR SER GLN ASN LEU CYS          
SEQRES   8 A  280  LEU LEU ALA LYS CYS PHE LEU ASP HIS ALY THR LEU TYR          
SEQRES   9 A  280  TYR ASP THR ASP PRO PHE LEU PHE TYR VAL MET THR GLU          
SEQRES  10 A  280  TYR ASP CYS LYS GLY PHE HIS ILE VAL GLY TYR PHE SER          
SEQRES  11 A  280  LYS GLU LYS GLU SER THR GLU ASP TYR ASN VAL ALA CYS          
SEQRES  12 A  280  ILE LEU THR LEU PRO PRO TYR GLN ARG ARG GLY TYR GLY          
SEQRES  13 A  280  LYS LEU LEU ILE GLU PHE SER TYR GLU LEU SER LYS VAL          
SEQRES  14 A  280  GLU GLY LYS THR GLY THR PRO GLU LYS PRO LEU SER ASP          
SEQRES  15 A  280  LEU GLY LEU LEU SER TYR ARG SER TYR TRP SER GLN THR          
SEQRES  16 A  280  ILE LEU GLU ILE LEU MET GLY LEU LYS SER GLU SER GLY          
SEQRES  17 A  280  GLU ARG PRO GLN ILE THR ILE ASN GLU ILE SER GLU ILE          
SEQRES  18 A  280  THR SER ILE LYS LYS GLU ASP VAL ILE SER THR LEU GLN          
SEQRES  19 A  280  TYR LEU ASN LEU ILE ASN TYR TYR LYS GLY GLN TYR ILE          
SEQRES  20 A  280  LEU THR LEU SER GLU ASP ILE VAL ASP GLY HIS GLU ARG          
SEQRES  21 A  280  ALA MET LEU LYS ARG LEU LEU ARG ILE ASP SER LYS CYS          
SEQRES  22 A  280  LEU HIS PHE THR PRO LYS ASP                                  
MODRES 2OU2 ALY A  275  LYS  N(6)-ACETYLLYSINE                                  
HET    ALY  A 275      12                                                       
HET     ZN  A 490       1                                                       
HET    ACO  A 500      51                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     ACO ACETYL COENZYME *A                                               
FORMUL   1  ALY    C8 H16 N2 O3                                                 
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  ACO    C23 H38 N7 O17 P3 S                                          
FORMUL   4  HOH   *30(H2 O)                                                     
HELIX    1   1 PRO A  199  THR A  203  5                                   5    
HELIX    2   2 SER A  220  CYS A  231  1                                  12    
HELIX    3   3 ASN A  257  CYS A  270  1                                  14    
HELIX    4   4 PRO A  322  GLN A  325  5                                   4    
HELIX    5   5 GLY A  328  GLU A  344  1                                  17    
HELIX    6   6 SER A  355  LEU A  374  1                                  20    
HELIX    7   7 ILE A  389  SER A  397  1                                   9    
HELIX    8   8 LYS A  399  LEU A  410  1                                  12    
HELIX    9   9 ASP A  444  LEU A  448  5                                   5    
SHEET    1   A 4 HIS A 188  LEU A 190  0                                        
SHEET    2   A 4 ILE A 183  LEU A 185 -1  N  ILE A 183   O  LEU A 190           
SHEET    3   A 4 LEU A 208  LEU A 210  1  O  LEU A 210   N  GLU A 184           
SHEET    4   A 4 TYR A 217  GLY A 218 -1  O  GLY A 218   N  TYR A 209           
SHEET    1   B 5 ASN A 239  LYS A 244  0                                        
SHEET    2   B 5 ILE A 247  ASP A 253 -1  O  GLU A 251   N  ASN A 239           
SHEET    3   B 5 PHE A 284  ASP A 293 -1  O  PHE A 286   N  ILE A 252           
SHEET    4   B 5 GLY A 296  GLU A 306 -1  O  HIS A 298   N  GLU A 291           
SHEET    5   B 5 ILE A 318  THR A 320 -1  O  LEU A 319   N  TYR A 302           
SHEET    1   C 2 TYR A 313  VAL A 315  0                                        
SHEET    2   C 2 THR A 349  PRO A 350  1  O  THR A 349   N  ASN A 314           
SHEET    1   D 2 ILE A 387  THR A 388  0                                        
SHEET    2   D 2 ILE A 421  LEU A 422 -1  O  LEU A 422   N  ILE A 387           
LINK         C   HIS A 274                 N   ALY A 275     1555   1555  1.33  
LINK         C   ALY A 275                 N   THR A 276     1555   1555  1.33  
LINK        ZN    ZN A 490                 SG  CYS A 214     1555   1555  2.18  
LINK        ZN    ZN A 490                 NE2 HIS A 227     1555   1555  2.13  
LINK        ZN    ZN A 490                 SG  CYS A 231     1555   1555  2.43  
LINK        ZN    ZN A 490                 SG  CYS A 211     1555   1555  2.32  
CISPEP   1 LYS A  352    PRO A  353          0         2.59                     
SITE     1 AC1  4 CYS A 211  CYS A 214  HIS A 227  CYS A 231                    
SITE     1 AC2 26 HOH A   1  HOH A   7  HOH A  25  ARG A 187                    
SITE     2 AC2 26 HIS A 188  ARG A 189  TRP A 193  PHE A 271                    
SITE     3 AC2 26 LEU A 272  ALA A 316  CYS A 317  ILE A 318                    
SITE     4 AC2 26 LEU A 319  THR A 320  GLN A 325  ARG A 326                    
SITE     5 AC2 26 ARG A 327  GLY A 328  GLY A 330  LYS A 331                    
SITE     6 AC2 26 GLU A 351  SER A 355  LEU A 357  SER A 361                    
SITE     7 AC2 26 SER A 364  GLN A 368                                          
CRYST1  107.632  107.632  133.731  90.00  90.00  90.00 I 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009291  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009291  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007478        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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