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Database: PDB
Entry: 5UEX
LinkDB: 5UEX
Original site: 5UEX 
HEADER    SIGNALING PROTEIN/INHIBITOR             03-JAN-17   5UEX              
TITLE     BRD4_BD2_A-1497627                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 352-457;                                          
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-PICHIA PASTORIS SHUTTLE VECTOR   
SOURCE   7 PPPARG4;                                                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1182032                                     
KEYWDS    SIGNALING PROTEIN-INHIBITOR COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.PARK                                                              
REVDAT   3   06-MAR-24 5UEX    1       REMARK                                   
REVDAT   2   24-MAY-17 5UEX    1       JRNL                                     
REVDAT   1   10-MAY-17 5UEX    0                                                
JRNL        AUTH   L.WANG,J.K.PRATT,T.SOLTWEDEL,G.S.SHEPPARD,S.D.FIDANZE,D.LIU, 
JRNL        AUTH 2 L.A.HASVOLD,R.A.MANTEI,J.H.HOLMS,W.J.MCCLELLAN,M.D.WENDT,    
JRNL        AUTH 3 C.WADA,R.FREY,T.M.HANSEN,R.HUBBARD,C.H.PARK,L.LI,T.J.MAGOC,  
JRNL        AUTH 4 D.H.ALBERT,X.LIN,S.E.WARDER,P.KOVAR,X.HUANG,D.WILCOX,R.WANG, 
JRNL        AUTH 5 G.RAJARAMAN,A.M.PETROS,C.W.HUTCHINS,S.C.PANCHAL,C.SUN,       
JRNL        AUTH 6 S.W.ELMORE,Y.SHEN,W.M.KATI,K.F.MCDANIEL                      
JRNL        TITL   FRAGMENT-BASED, STRUCTURE-ENABLED DISCOVERY OF NOVEL         
JRNL        TITL 2 PYRIDONES AND PYRIDONE MACROCYCLES AS POTENT BROMODOMAIN AND 
JRNL        TITL 3 EXTRA-TERMINAL DOMAIN (BET) FAMILY BROMODOMAIN INHIBITORS.   
JRNL        REF    J. MED. CHEM.                 V.  60  3828 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28368119                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 6154                           
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)  : 0.238                          
REMARK   3   R VALUE            (WORKING SET)  : 0.236                          
REMARK   3   FREE R VALUE                      : 0.279                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.650                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 286                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.020                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.29                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.56                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1704                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2940                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1617                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2920                   
REMARK   3   BIN FREE R VALUE                        : 0.3310                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.11                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 882                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -21.59950                                            
REMARK   3    B22 (A**2) : 19.33010                                             
REMARK   3    B33 (A**2) : 2.26940                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.400               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.478               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.275               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.381               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.258               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.887                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.847                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 966    ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 1323   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 322    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 20     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 149    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 966    ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 111    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 1154   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.67                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.11                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000224213.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-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               : 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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 2.11.7                         
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6417                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.9000                            
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: NULL                                                  
REMARK 200 STARTING MODEL: APO-BRD4_BD2                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER : 10 MM HEPES PH 7.5      
REMARK 280  100MM NACL, 5 MM DTT CRYSTALLIZATION : 15 % (V/V) ETHANOL, TRIS     
REMARK 280  PH 7.0, VAPOR DIFFUSION, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       26.12200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.21050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.12200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.21050            
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 6670 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 355    CD   CE   NZ                                        
REMARK 470     LYS A 378    CD   CE   NZ                                        
REMARK 470     GLN A 416    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 456       48.41    -86.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 89D A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UF0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UET   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UES   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UER   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UEW   RELATED DB: PDB                                   
DBREF  5UEX A  352   457  UNP    O60885   BRD4_HUMAN     352    457             
SEQADV 5UEX SER A  349  UNP  O60885              EXPRESSION TAG                 
SEQADV 5UEX HIS A  350  UNP  O60885              EXPRESSION TAG                 
SEQADV 5UEX MET A  351  UNP  O60885              EXPRESSION TAG                 
SEQRES   1 A  109  SER HIS MET GLU GLN LEU LYS CYS CYS SER GLY ILE LEU          
SEQRES   2 A  109  LYS GLU MET PHE ALA LYS LYS HIS ALA ALA TYR ALA TRP          
SEQRES   3 A  109  PRO PHE TYR LYS PRO VAL ASP VAL GLU ALA LEU GLY LEU          
SEQRES   4 A  109  HIS ASP TYR CYS ASP ILE ILE LYS HIS PRO MET ASP MET          
SEQRES   5 A  109  SER THR ILE LYS SER LYS LEU GLU ALA ARG GLU TYR ARG          
SEQRES   6 A  109  ASP ALA GLN GLU PHE GLY ALA ASP VAL ARG LEU MET PHE          
SEQRES   7 A  109  SER ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS GLU VAL          
SEQRES   8 A  109  VAL ALA MET ALA ARG LYS LEU GLN ASP VAL PHE GLU MET          
SEQRES   9 A  109  ARG PHE ALA LYS MET                                          
HET    89D  A 501      58                                                       
HETNAM     89D 17-{[ETHYL(DIHYDROXY)-LAMBDA~4~-SULFANYL]AMINO}-11,13-           
HETNAM   2 89D  DIFLUORO-2-METHYL-6,7,8,9-TETRAHYDRODIBENZO[4,5:7,              
HETNAM   3 89D  8][1,6]DIOXACYCLODODECINO[3,2-C]PYRIDIN-3(2H)-ONE               
FORMUL   2  89D    C24 H26 F2 N2 O5 S                                           
FORMUL   3  HOH   *93(H2 O)                                                     
HELIX    1 AA1 SER A  349  ALA A  366  1                                  18    
HELIX    2 AA2 HIS A  369  TRP A  374  1                                   6    
HELIX    3 AA3 PRO A  375  TYR A  377  5                                   3    
HELIX    4 AA4 ASP A  381  GLY A  386  1                                   6    
HELIX    5 AA5 ASP A  389  ILE A  394  1                                   6    
HELIX    6 AA6 ASP A  399  ALA A  409  1                                  11    
HELIX    7 AA7 ASP A  414  ASN A  433  1                                  20    
HELIX    8 AA8 HIS A  437  LYS A  456  1                                  20    
SITE     1 AC1 13 TRP A 374  PRO A 375  PHE A 376  LYS A 378                    
SITE     2 AC1 13 PRO A 379  VAL A 380  ASP A 381  LEU A 385                    
SITE     3 AC1 13 ASN A 433  HIS A 437  GLU A 438  VAL A 439                    
SITE     4 AC1 13 HOH A 601                                                     
CRYST1   52.244   74.421   33.333  90.00  90.00  90.00 P 21 21 2     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      0.019141  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013437  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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