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Database: PDB
Entry: 4O7B
LinkDB: 4O7B
Original site: 4O7B 
HEADER    TRANSCRIPTION/INHIBITOR                 24-DEC-13   4O7B              
TITLE     CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX   
TITLE    2 WITH SB-284847-BT                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 44-168;                                       
COMPND   5 SYNONYM: PROTEIN HUNK1;                                              
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: BRD4, HUNK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    BROMODOMAIN, CAP, HUNK1, MCAP, PROTEIN BINDING-INHIBITOR COMPLEX,     
KEYWDS   2 MITOTIC CHROMOSOME ASSOCIATED PROTEIN, CELL CYCLE, INHIBITOR,        
KEYWDS   3 TRANSCRIPTION-INHIBITOR COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.EMBER,J.-Y.ZHU,C.WATTS,E.SCHONBRUNN                               
REVDAT   4   20-SEP-23 4O7B    1       REMARK SEQADV                            
REVDAT   3   28-MAY-14 4O7B    1       JRNL                                     
REVDAT   2   19-MAR-14 4O7B    1       JRNL                                     
REVDAT   1   05-MAR-14 4O7B    0                                                
JRNL        AUTH   S.W.EMBER,J.Y.ZHU,S.H.OLESEN,M.P.MARTIN,A.BECKER,N.BERNDT,   
JRNL        AUTH 2 G.I.GEORG,E.SCHONBRUNN                                       
JRNL        TITL   ACETYL-LYSINE BINDING SITE OF BROMODOMAIN-CONTAINING PROTEIN 
JRNL        TITL 2 4 (BRD4) INTERACTS WITH DIVERSE KINASE INHIBITORS.           
JRNL        REF    ACS CHEM.BIOL.                V.   9  1160 2014              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   24568369                                                     
JRNL        DOI    10.1021/CB500072Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 21468                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.180                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 26.8158 -  3.6148    1.00     1506   156  0.1665 0.1879        
REMARK   3     2  3.6148 -  2.8703    1.00     1428   146  0.1667 0.2090        
REMARK   3     3  2.8703 -  2.5077    1.00     1404   144  0.1573 0.1783        
REMARK   3     4  2.5077 -  2.2786    1.00     1415   145  0.1413 0.1829        
REMARK   3     5  2.2786 -  2.1153    1.00     1388   143  0.1252 0.1477        
REMARK   3     6  2.1153 -  1.9907    1.00     1372   141  0.1303 0.1679        
REMARK   3     7  1.9907 -  1.8910    1.00     1387   142  0.1315 0.1844        
REMARK   3     8  1.8910 -  1.8087    1.00     1371   141  0.1228 0.1716        
REMARK   3     9  1.8087 -  1.7391    1.00     1383   142  0.1267 0.1579        
REMARK   3    10  1.7391 -  1.6791    1.00     1367   140  0.1142 0.1824        
REMARK   3    11  1.6791 -  1.6266    1.00     1360   140  0.1051 0.1581        
REMARK   3    12  1.6266 -  1.5801    1.00     1375   141  0.1068 0.1627        
REMARK   3    13  1.5801 -  1.5385    1.00     1371   140  0.1100 0.1829        
REMARK   3    14  1.5385 -  1.5000    1.00     1341   139  0.1217 0.1962        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.050           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.009           1138                                  
REMARK   3   ANGLE     :  1.254           1544                                  
REMARK   3   CHIRALITY :  0.067            159                                  
REMARK   3   PLANARITY :  0.008            197                                  
REMARK   3   DIHEDRAL  : 14.275            451                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4O7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084132.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21519                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OSS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5 MG/ML BRD4, 5MM HEPES PH 7.5,       
REMARK 280  50MM SODIUM CHLORIDE, 0.5MM DTT, 50MM TRIS PH8.5, 0.1M AMMONIUM     
REMARK 280  SULFATE, 12.5% PEG 3,350, 10% DMSO, 1 MM SB-284847-BT, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       18.72400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.44250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.98350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.44250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.72400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.98350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 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 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   HD1  HIS A    77     H    PHE A    79              1.34            
REMARK 500   O1   EDO A   203     O    HOH A   341              2.15            
REMARK 500   O    HOH A   388     O    HOH A   389              2.17            
REMARK 500   O    HOH A   370     O    HOH A   429              2.17            
REMARK 500   O    HOH A   404     O    HOH A   417              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH A   386     O    HOH A   422     4455     2.18            
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    ASN A  52       96.19   -165.42                                   
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 2RJ A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 204                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O70   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O71   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O72   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O74   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O75   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O76   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O77   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O78   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O7A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O7C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O7E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O7F   RELATED DB: PDB                                   
DBREF  4O7B A   44   168  UNP    O60885   BRD4_HUMAN      44    168             
SEQADV 4O7B SER A   42  UNP  O60885              EXPRESSION TAG                 
SEQADV 4O7B MET A   43  UNP  O60885              EXPRESSION TAG                 
SEQRES   1 A  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 A  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 A  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 A  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 A  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 A  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 A  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 A  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 A  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 A  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
HET    2RJ  A 201      59                                                       
HET    EDO  A 202      10                                                       
HET    EDO  A 203      10                                                       
HET    EDO  A 204      10                                                       
HETNAM     2RJ 2-(2,3-DIMETHYLPHENOXY)-4-[4-(4-FLUOROPHENYL)-1-                 
HETNAM   2 2RJ  (PIPERIDIN-4-YL)-1H-IMIDAZOL-5-YL]PYRIMIDINE                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  2RJ    C26 H26 F N5 O                                               
FORMUL   3  EDO    3(C2 H6 O2)                                                  
FORMUL   6  HOH   *136(H2 O)                                                    
HELIX    1   1 THR A   60  VAL A   69  1                                  10    
HELIX    2   2 VAL A   69  LYS A   76  1                                   8    
HELIX    3   3 ALA A   80  GLN A   84  5                                   5    
HELIX    4   4 ASP A   96  ILE A  101  1                                   6    
HELIX    5   5 ASP A  106  ASN A  116  1                                  11    
HELIX    6   6 ASN A  121  ASN A  140  1                                  20    
HELIX    7   7 ASP A  144  ASN A  162  1                                  19    
SITE     1 AC1 14 TRP A  81  PRO A  82  PHE A  83  LEU A  92                    
SITE     2 AC1 14 LEU A  94  TYR A  97  LYS A  99  MET A 132                    
SITE     3 AC1 14 ASN A 140  ASP A 145  ILE A 146  HOH A 356                    
SITE     4 AC1 14 HOH A 410  HOH A 414                                          
SITE     1 AC2  5 ILE A 100  ILE A 101  LYS A 102  THR A 103                    
SITE     2 AC2  5 ASN A 135                                                     
SITE     1 AC3  6 LEU A  63  GLN A  64  LEU A  67  LEU A 114                    
SITE     2 AC3  6 HOH A 341  HOH A 360                                          
SITE     1 AC4  4 ARG A  68  GLY A 143  VAL A 147  GLU A 151                    
CRYST1   37.448   43.967   78.885  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026704  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022744  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012677        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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