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Database: PDB
Entry: 6BOY
LinkDB: 6BOY
Original site: 6BOY 
HEADER    LIGASE                                  21-NOV-17   6BOY              
TITLE     CRYSTAL STRUCTURE OF DDB1-CRBN-BRD4(BD1) COMPLEX BOUND TO DBET6       
TITLE    2 PROTAC.                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DDB P127 SUBUNIT,DNA DAMAGE-BINDING PROTEIN A,DDBA,DAMAGE-  
COMPND   5 SPECIFIC DNA-BINDING PROTEIN 1,HBV X-ASSOCIATED PROTEIN 1,XAP-1,UV-  
COMPND   6 DAMAGED DNA-BINDING FACTOR,UV-DAMAGED DNA-BINDING PROTEIN 1,UV-DDB 1,
COMPND   7 XPE-BINDING FACTOR,XPE-BF,XERODERMA PIGMENTOSUM GROUP E-COMPLEMENTING
COMPND   8 PROTEIN,XPCE,DDB P127 SUBUNIT,DNA DAMAGE-BINDING PROTEIN A,DDBA,     
COMPND   9 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1,HBV X-ASSOCIATED PROTEIN 1,XAP-
COMPND  10 1,UV-DAMAGED DNA-BINDING FACTOR,UV-DAMAGED DNA-BINDING PROTEIN 1,UV- 
COMPND  11 DDB 1,XPE-BINDING FACTOR,XPE-BF,XERODERMA PIGMENTOSUM GROUP E-       
COMPND  12 COMPLEMENTING PROTEIN,XPCE;                                          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 2;                                                           
COMPND  15 MOLECULE: PROTEIN CEREBLON;                                          
COMPND  16 CHAIN: B;                                                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 3;                                                           
COMPND  19 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND  20 CHAIN: C;                                                            
COMPND  21 FRAGMENT: RESIDUES 42-168;                                           
COMPND  22 SYNONYM: PROTEIN HUNK1;                                              
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDB1, XAP1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CRBN, AD-006;                                                  
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: BRD4, HUNK1;                                                   
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTAC, DEGRADER, E3 LIGASE, CRBN, LIGASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.P.NOWAK,S.L.DEANGELO,D.BUCKLEY,J.E.BRADNER,E.S.FISCHER              
REVDAT   6   04-OCT-23 6BOY    1       REMARK                                   
REVDAT   5   04-DEC-19 6BOY    1       REMARK                                   
REVDAT   4   20-FEB-19 6BOY    1       REMARK                                   
REVDAT   3   07-NOV-18 6BOY    1       JRNL                                     
REVDAT   2   01-AUG-18 6BOY    1       JRNL                                     
REVDAT   1   30-MAY-18 6BOY    0                                                
JRNL        AUTH   R.P.NOWAK,S.L.DEANGELO,D.BUCKLEY,Z.HE,K.A.DONOVAN,J.AN,      
JRNL        AUTH 2 N.SAFAEE,M.P.JEDRYCHOWSKI,C.M.PONTHIER,M.ISHOEY,T.ZHANG,     
JRNL        AUTH 3 J.D.MANCIAS,N.S.GRAY,J.E.BRADNER,E.S.FISCHER                 
JRNL        TITL   PLASTICITY IN BINDING CONFERS SELECTIVITY IN LIGAND-INDUCED  
JRNL        TITL 2 PROTEIN DEGRADATION.                                         
JRNL        REF    NAT. CHEM. BIOL.              V.  14   706 2018              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   29892083                                                     
JRNL        DOI    10.1038/S41589-018-0055-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 35242                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.220                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1839                            
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 49.7984 -  7.8207    1.00     2864   182  0.1916 0.2078        
REMARK   3     2  7.8207 -  6.2113    1.00     2667   156  0.2162 0.2484        
REMARK   3     3  6.2113 -  5.4272    1.00     2627   139  0.2072 0.2305        
REMARK   3     4  5.4272 -  4.9315    1.00     2600   139  0.1729 0.2485        
REMARK   3     5  4.9315 -  4.5783    1.00     2555   149  0.1548 0.2088        
REMARK   3     6  4.5783 -  4.3085    1.00     2558   140  0.1588 0.1910        
REMARK   3     7  4.3085 -  4.0928    1.00     2518   155  0.1811 0.2159        
REMARK   3     8  4.0928 -  3.9148    1.00     2553   133  0.2175 0.2803        
REMARK   3     9  3.9148 -  3.7641    1.00     2549   121  0.2332 0.2872        
REMARK   3    10  3.7641 -  3.6343    1.00     2500   132  0.2471 0.2866        
REMARK   3    11  3.6343 -  3.5207    1.00     2546   133  0.2691 0.3218        
REMARK   3    12  3.5207 -  3.4200    1.00     2495   138  0.3068 0.4036        
REMARK   3    13  3.4200 -  3.3300    0.94     2371   122  0.3859 0.4343        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.350           
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      :  0.002          10593                                  
REMARK   3   ANGLE     :  0.500          14379                                  
REMARK   3   CHIRALITY :  0.043           1622                                  
REMARK   3   PLANARITY :  0.004           1892                                  
REMARK   3   DIHEDRAL  :  3.267           6401                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  70.8418  53.7786   8.2940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5978 T22:   1.5331                                     
REMARK   3      T33:   1.3177 T12:   0.0451                                     
REMARK   3      T13:  -0.0224 T23:   0.3916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3109 L22:   0.9934                                     
REMARK   3      L33:   1.8784 L12:   0.5581                                     
REMARK   3      L13:  -0.4725 L23:  -0.4121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1250 S12:   0.4168 S13:   0.2096                       
REMARK   3      S21:   0.0411 S22:   0.0525 S23:   0.0312                       
REMARK   3      S31:  -0.2016 S32:   0.2958 S33:   0.0706                       
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 6BOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231151.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35541                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.793                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 32.20                              
REMARK 200  R MERGE                    (I) : 0.17900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 33.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 5.47100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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: 6BN7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) PEG20K, 18% (V/V) PEG MME       
REMARK 280  550, 0.09M BICINE PH8.5, 9% (V/V) SILVER BULLET D11 (0.25% W/V 2,   
REMARK 280  6-NAPHTHALENEDISULFONIC ACID DISODIUM SALT, 0.25% W/V 4-            
REMARK 280  AMINOBENZOIC ACID, 0.25% W/V 5-SULFOSALICYLIC ACID DIHYDRATE,       
REMARK 280  0.25% W/V NAPHTHALENE-1,3,6-TRISULFONIC ACID TRISODIUM SALT         
REMARK 280  HYDRATE, 0.02 M HEPES SODIUM PH 6.8), VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      392.09533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      196.04767            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      294.07150            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       98.02383            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      490.11917            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      392.09533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      196.04767            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       98.02383            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      294.07150            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      490.11917            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 55700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   -27                                                      
REMARK 465     GLY A   -26                                                      
REMARK 465     SER A   -25                                                      
REMARK 465     SER A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     ALA A   -16                                                      
REMARK 465     ALA A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     MET A   -11                                                      
REMARK 465     VAL A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     THR A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     GLU A   289                                                      
REMARK 465     GLN A   290                                                      
REMARK 465     MET A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     ILE A   698                                                      
REMARK 465     GLY A   699                                                      
REMARK 465     GLY A   700                                                      
REMARK 465     ASN A   701                                                      
REMARK 465     GLY A   702                                                      
REMARK 465     ASN A   703                                                      
REMARK 465     SER A   704                                                      
REMARK 465     GLY A   705                                                      
REMARK 465     GLU A   706                                                      
REMARK 465     ILE A   707                                                      
REMARK 465     GLN A   708                                                      
REMARK 465     PHE A   771                                                      
REMARK 465     SER A   772                                                      
REMARK 465     SER A   773                                                      
REMARK 465     SER A   774                                                      
REMARK 465     THR A   775                                                      
REMARK 465     ASN A  1016                                                      
REMARK 465     LEU A  1017                                                      
REMARK 465     GLY A  1018                                                      
REMARK 465     GLU A  1019                                                      
REMARK 465     THR A  1020                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     ALA B    -9                                                      
REMARK 465     VAL B    -8                                                      
REMARK 465     ASP B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PHE B    -2                                                      
REMARK 465     GLN B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     ASN B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     MET B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     ASP B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     LYS B    42                                                      
REMARK 465     LYS B    43                                                      
REMARK 465     SER B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     PRO B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     ASP B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     THR B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     ASP B   431                                                      
REMARK 465     GLU B   432                                                      
REMARK 465     ILE B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     PRO B   435                                                      
REMARK 465     ASP B   436                                                      
REMARK 465     LYS B   437                                                      
REMARK 465     VAL B   438                                                      
REMARK 465     ILE B   439                                                      
REMARK 465     LEU B   440                                                      
REMARK 465     CYS B   441                                                      
REMARK 465     LEU B   442                                                      
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     GLU A  27    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     ASP A  99    CG   OD1  OD2                                       
REMARK 470     ARG A 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 147    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     GLN A 186    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 204    CG   CD   CE   NZ                                   
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     GLN A 209    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 237    CG1  CG2  CD1                                       
REMARK 470     LYS A 287    CG   CD   CE   NZ                                   
REMARK 470     LYS A 298    CG   CD   CE   NZ                                   
REMARK 470     VAL A 338    CG1  CG2                                            
REMARK 470     ARG A 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 709    CG   CD   CE   NZ                                   
REMARK 470     LYS A 769    CG   CD   CE   NZ                                   
REMARK 470     LYS A 823    CG   CD   CE   NZ                                   
REMARK 470     LYS A 867    CG   CD   CE   NZ                                   
REMARK 470     SER A 981    OG                                                  
REMARK 470     GLN A1113    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1121    CG   CD   CE   NZ                                   
REMARK 470     LYS A1131    CG   CD   CE   NZ                                   
REMARK 470     ASN B  45    CG   OD1  ND2                                       
REMARK 470     ARG B  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 269    CG   CD   CE   NZ                                   
REMARK 470     TYR B 363    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 141    CD   CE   NZ                                        
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    TYR A   3       71.45     58.06                                   
REMARK 500    ASN A  36      -89.16     55.08                                   
REMARK 500    LEU A 145       52.70    -90.48                                   
REMARK 500    VAL A 212     -169.29   -112.91                                   
REMARK 500    ASN A 241       85.89   -165.70                                   
REMARK 500    VAL A 264      -70.58    -92.32                                   
REMARK 500    ILE A 310       97.63    -57.19                                   
REMARK 500    LEU A 317      -89.19    -89.18                                   
REMARK 500    ASN A 341     -156.89    -78.75                                   
REMARK 500    LEU A 367      -76.54    -66.27                                   
REMARK 500    GLU A 368      -97.18    -71.25                                   
REMARK 500    PHE A 382     -137.85     61.84                                   
REMARK 500    SER A 746      -99.28    -78.00                                   
REMARK 500    SER A 755     -168.53   -116.09                                   
REMARK 500    THR A 780     -174.59     57.53                                   
REMARK 500    ASN A 885     -117.54     52.27                                   
REMARK 500    LYS A 917      111.98   -161.85                                   
REMARK 500    MET A 927       42.24   -101.56                                   
REMARK 500    ASN A 952      145.68   -170.45                                   
REMARK 500    SER A 955      -31.71   -153.35                                   
REMARK 500    GLU A 969     -156.24   -138.92                                   
REMARK 500    ALA A 983     -154.89     56.21                                   
REMARK 500    THR A 984      -31.05   -137.11                                   
REMARK 500    SER A1027      114.22   -164.16                                   
REMARK 500    PHE A1076      103.54    -56.27                                   
REMARK 500    GLU A1079        0.32    -69.15                                   
REMARK 500    LEU A1112     -103.88    -74.51                                   
REMARK 500    ASP A1116       59.17   -119.43                                   
REMARK 500    MET A1120     -129.54   -108.45                                   
REMARK 500    ARG A1138       11.74    -68.88                                   
REMARK 500    ASN B  45     -167.78     59.13                                   
REMARK 500    ASP B  50       96.11     66.25                                   
REMARK 500    ASP B  76       -4.28     64.65                                   
REMARK 500    LYS B 116     -130.07   -115.74                                   
REMARK 500    ARG B 145      113.31   -160.14                                   
REMARK 500    GLN B 148     -155.28    -87.78                                   
REMARK 500    ASP B 149       38.49     28.30                                   
REMARK 500    ARG B 162      -71.08   -118.49                                   
REMARK 500    CYS B 234       -3.86    -59.53                                   
REMARK 500    ASP B 271      -40.36   -138.75                                   
REMARK 500    GLN B 327       -9.82     66.29                                   
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 B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 323   SG                                                     
REMARK 620 2 CYS B 326   SG  116.1                                              
REMARK 620 3 CYS B 391   SG  136.8  95.4                                        
REMARK 620 4 CYS B 394   SG  101.5  94.7 104.8                                  
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 B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RN6 B 502                 
DBREF  6BOY A    1   699  UNP    Q16531   DDB1_HUMAN       1    395             
DBREF  6BOY A  706  1140  UNP    Q16531   DDB1_HUMAN     706   1140             
DBREF  6BOY B    2   442  UNP    Q96SW2   CRBN_HUMAN       1    441             
DBREF  6BOY C   42   168  UNP    O60885   BRD4_HUMAN      42    168             
SEQADV 6BOY MET A  -27  UNP  Q16531              INITIATING METHIONINE          
SEQADV 6BOY GLY A  -26  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY SER A  -25  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY SER A  -24  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -23  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -22  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -21  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -20  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -19  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -18  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY SER A  -17  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ALA A  -16  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ALA A  -15  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY HIS A  -14  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ILE A  -13  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY VAL A  -12  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY MET A  -11  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY VAL A  -10  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ASP A   -9  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ALA A   -8  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY TYR A   -7  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY LYS A   -6  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY PRO A   -5  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY THR A   -4  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY LYS A   -3  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY GLY A   -2  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY GLY A   -1  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY ARG A    0  UNP  Q16531              EXPRESSION TAG                 
SEQADV 6BOY GLY A  700  UNP  Q16531              LINKER                         
SEQADV 6BOY ASN A  701  UNP  Q16531              LINKER                         
SEQADV 6BOY GLY A  702  UNP  Q16531              LINKER                         
SEQADV 6BOY ASN A  703  UNP  Q16531              LINKER                         
SEQADV 6BOY SER A  704  UNP  Q16531              LINKER                         
SEQADV 6BOY GLY A  705  UNP  Q16531              LINKER                         
SEQADV 6BOY MET B  -20  UNP  Q96SW2              INITIATING METHIONINE          
SEQADV 6BOY GLY B  -19  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY SER B  -18  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY SER B  -17  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -16  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -15  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -14  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -13  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -12  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY HIS B  -11  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY SER B  -10  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY ALA B   -9  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY VAL B   -8  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY ASP B   -7  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY GLU B   -6  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY ASN B   -5  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY LEU B   -4  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY TYR B   -3  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY PHE B   -2  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY GLN B   -1  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY GLY B    0  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY GLY B    1  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 6BOY MET C   43  UNP  O60885    THR    43 ENGINEERED MUTATION            
SEQRES   1 A  864  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA ALA          
SEQRES   2 A  864  HIS ILE VAL MET VAL ASP ALA TYR LYS PRO THR LYS GLY          
SEQRES   3 A  864  GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA GLN LYS          
SEQRES   4 A  864  PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS PHE THR          
SEQRES   5 A  864  SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS ASN THR          
SEQRES   6 A  864  ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY LEU ARG          
SEQRES   7 A  864  PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE ALA VAL          
SEQRES   8 A  864  MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS ASP LEU          
SEQRES   9 A  864  LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS ILE LEU          
SEQRES  10 A  864  GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE ILE THR          
SEQRES  11 A  864  ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY ARG PRO          
SEQRES  12 A  864  SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO GLU CYS          
SEQRES  13 A  864  ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU PHE LYS          
SEQRES  14 A  864  VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU LYS ALA          
SEQRES  15 A  864  PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE ASP VAL          
SEQRES  16 A  864  LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE CYS PHE          
SEQRES  17 A  864  VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS THR TYR          
SEQRES  18 A  864  GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS GLY PRO          
SEQRES  19 A  864  TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER MET VAL          
SEQRES  20 A  864  ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE ILE ILE          
SEQRES  21 A  864  GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP LYS TYR          
SEQRES  22 A  864  LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER THR ILE          
SEQRES  23 A  864  VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER ARG TYR          
SEQRES  24 A  864  LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET LEU LEU          
SEQRES  25 A  864  LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL THR LEU          
SEQRES  26 A  864  LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR SER ILE          
SEQRES  27 A  864  ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL VAL PHE          
SEQRES  28 A  864  VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL LYS LEU          
SEQRES  29 A  864  ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL VAL ALA          
SEQRES  30 A  864  MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL ASP MET          
SEQRES  31 A  864  CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY GLN LEU          
SEQRES  32 A  864  VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER LEU ARG          
SEQRES  33 A  864  ILE ILE ARG ASN GLY ILE GLY GLY ASN GLY ASN SER GLY          
SEQRES  34 A  864  GLU ILE GLN LYS LEU HIS ILE ARG THR VAL PRO LEU TYR          
SEQRES  35 A  864  GLU SER PRO ARG LYS ILE CYS TYR GLN GLU VAL SER GLN          
SEQRES  36 A  864  CYS PHE GLY VAL LEU SER SER ARG ILE GLU VAL GLN ASP          
SEQRES  37 A  864  THR SER GLY GLY THR THR ALA LEU ARG PRO SER ALA SER          
SEQRES  38 A  864  THR GLN ALA LEU SER SER SER VAL SER SER SER LYS LEU          
SEQRES  39 A  864  PHE SER SER SER THR ALA PRO HIS GLU THR SER PHE GLY          
SEQRES  40 A  864  GLU GLU VAL GLU VAL HIS ASN LEU LEU ILE ILE ASP GLN          
SEQRES  41 A  864  HIS THR PHE GLU VAL LEU HIS ALA HIS GLN PHE LEU GLN          
SEQRES  42 A  864  ASN GLU TYR ALA LEU SER LEU VAL SER CYS LYS LEU GLY          
SEQRES  43 A  864  LYS ASP PRO ASN THR TYR PHE ILE VAL GLY THR ALA MET          
SEQRES  44 A  864  VAL TYR PRO GLU GLU ALA GLU PRO LYS GLN GLY ARG ILE          
SEQRES  45 A  864  VAL VAL PHE GLN TYR SER ASP GLY LYS LEU GLN THR VAL          
SEQRES  46 A  864  ALA GLU LYS GLU VAL LYS GLY ALA VAL TYR SER MET VAL          
SEQRES  47 A  864  GLU PHE ASN GLY LYS LEU LEU ALA SER ILE ASN SER THR          
SEQRES  48 A  864  VAL ARG LEU TYR GLU TRP THR THR GLU LYS GLU LEU ARG          
SEQRES  49 A  864  THR GLU CYS ASN HIS TYR ASN ASN ILE MET ALA LEU TYR          
SEQRES  50 A  864  LEU LYS THR LYS GLY ASP PHE ILE LEU VAL GLY ASP LEU          
SEQRES  51 A  864  MET ARG SER VAL LEU LEU LEU ALA TYR LYS PRO MET GLU          
SEQRES  52 A  864  GLY ASN PHE GLU GLU ILE ALA ARG ASP PHE ASN PRO ASN          
SEQRES  53 A  864  TRP MET SER ALA VAL GLU ILE LEU ASP ASP ASP ASN PHE          
SEQRES  54 A  864  LEU GLY ALA GLU ASN ALA PHE ASN LEU PHE VAL CYS GLN          
SEQRES  55 A  864  LYS ASP SER ALA ALA THR THR ASP GLU GLU ARG GLN HIS          
SEQRES  56 A  864  LEU GLN GLU VAL GLY LEU PHE HIS LEU GLY GLU PHE VAL          
SEQRES  57 A  864  ASN VAL PHE CYS HIS GLY SER LEU VAL MET GLN ASN LEU          
SEQRES  58 A  864  GLY GLU THR SER THR PRO THR GLN GLY SER VAL LEU PHE          
SEQRES  59 A  864  GLY THR VAL ASN GLY MET ILE GLY LEU VAL THR SER LEU          
SEQRES  60 A  864  SER GLU SER TRP TYR ASN LEU LEU LEU ASP MET GLN ASN          
SEQRES  61 A  864  ARG LEU ASN LYS VAL ILE LYS SER VAL GLY LYS ILE GLU          
SEQRES  62 A  864  HIS SER PHE TRP ARG SER PHE HIS THR GLU ARG LYS THR          
SEQRES  63 A  864  GLU PRO ALA THR GLY PHE ILE ASP GLY ASP LEU ILE GLU          
SEQRES  64 A  864  SER PHE LEU ASP ILE SER ARG PRO LYS MET GLN GLU VAL          
SEQRES  65 A  864  VAL ALA ASN LEU GLN TYR ASP ASP GLY SER GLY MET LYS          
SEQRES  66 A  864  ARG GLU ALA THR ALA ASP ASP LEU ILE LYS VAL VAL GLU          
SEQRES  67 A  864  GLU LEU THR ARG ILE HIS                                      
SEQRES   1 B  463  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA VAL          
SEQRES   2 B  463  ASP GLU ASN LEU TYR PHE GLN GLY GLY MET ALA GLY GLU          
SEQRES   3 B  463  GLY ASP GLN GLN ASP ALA ALA HIS ASN MET GLY ASN HIS          
SEQRES   4 B  463  LEU PRO LEU LEU PRO GLU SER GLU GLU GLU ASP GLU MET          
SEQRES   5 B  463  GLU VAL GLU ASP GLN ASP SER LYS GLU ALA LYS LYS PRO          
SEQRES   6 B  463  ASN ILE ILE ASN PHE ASP THR SER LEU PRO THR SER HIS          
SEQRES   7 B  463  THR TYR LEU GLY ALA ASP MET GLU GLU PHE HIS GLY ARG          
SEQRES   8 B  463  THR LEU HIS ASP ASP ASP SER CYS GLN VAL ILE PRO VAL          
SEQRES   9 B  463  LEU PRO GLN VAL MET MET ILE LEU ILE PRO GLY GLN THR          
SEQRES  10 B  463  LEU PRO LEU GLN LEU PHE HIS PRO GLN GLU VAL SER MET          
SEQRES  11 B  463  VAL ARG ASN LEU ILE GLN LYS ASP ARG THR PHE ALA VAL          
SEQRES  12 B  463  LEU ALA TYR SER ASN VAL GLN GLU ARG GLU ALA GLN PHE          
SEQRES  13 B  463  GLY THR THR ALA GLU ILE TYR ALA TYR ARG GLU GLU GLN          
SEQRES  14 B  463  ASP PHE GLY ILE GLU ILE VAL LYS VAL LYS ALA ILE GLY          
SEQRES  15 B  463  ARG GLN ARG PHE LYS VAL LEU GLU LEU ARG THR GLN SER          
SEQRES  16 B  463  ASP GLY ILE GLN GLN ALA LYS VAL GLN ILE LEU PRO GLU          
SEQRES  17 B  463  CYS VAL LEU PRO SER THR MET SER ALA VAL GLN LEU GLU          
SEQRES  18 B  463  SER LEU ASN LYS CYS GLN ILE PHE PRO SER LYS PRO VAL          
SEQRES  19 B  463  SER ARG GLU ASP GLN CYS SER TYR LYS TRP TRP GLN LYS          
SEQRES  20 B  463  TYR GLN LYS ARG LYS PHE HIS CYS ALA ASN LEU THR SER          
SEQRES  21 B  463  TRP PRO ARG TRP LEU TYR SER LEU TYR ASP ALA GLU THR          
SEQRES  22 B  463  LEU MET ASP ARG ILE LYS LYS GLN LEU ARG GLU TRP ASP          
SEQRES  23 B  463  GLU ASN LEU LYS ASP ASP SER LEU PRO SER ASN PRO ILE          
SEQRES  24 B  463  ASP PHE SER TYR ARG VAL ALA ALA CYS LEU PRO ILE ASP          
SEQRES  25 B  463  ASP VAL LEU ARG ILE GLN LEU LEU LYS ILE GLY SER ALA          
SEQRES  26 B  463  ILE GLN ARG LEU ARG CYS GLU LEU ASP ILE MET ASN LYS          
SEQRES  27 B  463  CYS THR SER LEU CYS CYS LYS GLN CYS GLN GLU THR GLU          
SEQRES  28 B  463  ILE THR THR LYS ASN GLU ILE PHE SER LEU SER LEU CYS          
SEQRES  29 B  463  GLY PRO MET ALA ALA TYR VAL ASN PRO HIS GLY TYR VAL          
SEQRES  30 B  463  HIS GLU THR LEU THR VAL TYR LYS ALA CYS ASN LEU ASN          
SEQRES  31 B  463  LEU ILE GLY ARG PRO SER THR GLU HIS SER TRP PHE PRO          
SEQRES  32 B  463  GLY TYR ALA TRP THR VAL ALA GLN CYS LYS ILE CYS ALA          
SEQRES  33 B  463  SER HIS ILE GLY TRP LYS PHE THR ALA THR LYS LYS ASP          
SEQRES  34 B  463  MET SER PRO GLN LYS PHE TRP GLY LEU THR ARG SER ALA          
SEQRES  35 B  463  LEU LEU PRO THR ILE PRO ASP THR GLU ASP GLU ILE SER          
SEQRES  36 B  463  PRO ASP LYS VAL ILE LEU CYS LEU                              
SEQRES   1 C  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 C  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 C  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 C  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 C  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 C  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 C  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 C  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 C  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 C  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
HET     ZN  B 501       1                                                       
HET    RN6  B 502      59                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     RN6 2-[(6S)-4-(4-CHLOROPHENYL)-2,3,9-TRIMETHYL-6H-THIENO[3,          
HETNAM   2 RN6  2-F][1,2,4]TRIAZOLO[4,3-A][1,4]DIAZEPIN-6-YL]-N-(8-             
HETNAM   3 RN6  {[({2-[(3S)-2,6-DIOXOPIPERIDIN-3-YL]-1,3-DIOXO-2,3-             
HETNAM   4 RN6  DIHYDRO-1H-ISOINDOL-4-YL}OXY)ACETYL]AMINO}OCTYL)                
HETNAM   5 RN6  ACETAMIDE                                                       
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  RN6    C42 H45 CL N8 O7 S                                           
HELIX    1 AA1 PRO A  250  GLN A  255  5                                   6    
HELIX    2 AA2 ALA A  381  GLU A  384  5                                   4    
HELIX    3 AA3 GLU A  728  SER A  730  5                                   3    
HELIX    4 AA4 SER A  755  GLN A  759  5                                   5    
HELIX    5 AA5 THR A  985  GLN A  990  1                                   6    
HELIX    6 AA6 SER A 1044  LYS A 1060  1                                  17    
HELIX    7 AA7 GLU A 1069  SER A 1075  1                                   7    
HELIX    8 AA8 GLY A 1091  SER A 1096  1                                   6    
HELIX    9 AA9 PHE A 1097  ILE A 1100  5                                   4    
HELIX   10 AB1 SER A 1101  ALA A 1110  1                                  10    
HELIX   11 AB2 THR A 1125  ARG A 1138  1                                  14    
HELIX   12 AB3 THR B   51  HIS B   57  1                                   7    
HELIX   13 AB4 THR B   58  GLY B   61  5                                   4    
HELIX   14 AB5 HIS B  103  LYS B  116  1                                  14    
HELIX   15 AB6 LEU B  202  GLN B  206  5                                   5    
HELIX   16 AB7 SER B  220  PHE B  232  1                                  13    
HELIX   17 AB8 HIS B  233  THR B  238  5                                   6    
HELIX   18 AB9 PRO B  241  LEU B  247  1                                   7    
HELIX   19 AC1 ASP B  249  GLU B  263  1                                  15    
HELIX   20 AC2 ASN B  276  CYS B  287  1                                  12    
HELIX   21 AC3 ASP B  291  ILE B  301  1                                  11    
HELIX   22 AC4 SER B  303  CYS B  318  1                                  16    
HELIX   23 AC5 ASN B  335  ILE B  337  5                                   3    
HELIX   24 AC6 THR C   60  VAL C   69  1                                  10    
HELIX   25 AC7 VAL C   69  LYS C   76  1                                   8    
HELIX   26 AC8 ALA C   80  GLN C   84  5                                   5    
HELIX   27 AC9 ASP C   96  ILE C  101  1                                   6    
HELIX   28 AD1 ASP C  106  ASN C  116  1                                  11    
HELIX   29 AD2 ASN C  121  ASN C  140  1                                  20    
HELIX   30 AD3 ASP C  144  ASN C  162  1                                  19    
SHEET    1 AA1 5 VAL A1004  HIS A1009  0                                        
SHEET    2 AA1 5 GLN A1025  THR A1032 -1  O  GLY A1031   N  ASN A1005           
SHEET    3 AA1 5 ILE A1037  SER A1042 -1  O  GLY A1038   N  PHE A1030           
SHEET    4 AA1 5 ASN A   4  GLN A  10 -1  N  VAL A   7   O  LEU A1039           
SHEET    5 AA1 5 PHE A1088  ASP A1090  1  O  ILE A1089   N  VAL A   6           
SHEET    1 AA2 4 GLY A  17  GLY A  21  0                                        
SHEET    2 AA2 4 ASN A  30  ALA A  34 -1  O  LEU A  32   N  VAL A  19           
SHEET    3 AA2 4 ARG A  38  VAL A  44 -1  O  GLU A  40   N  ILE A  33           
SHEET    4 AA2 4 LEU A  49  GLY A  56 -1  O  VAL A  52   N  ILE A  41           
SHEET    1 AA3 4 ILE A  61  PHE A  67  0                                        
SHEET    2 AA3 4 LEU A  76  THR A  81 -1  O  LEU A  76   N  PHE A  67           
SHEET    3 AA3 4 ASN A  85  SER A  94 -1  O  LEU A  89   N  LEU A  77           
SHEET    4 AA3 4 SER A  97  ASN A 107 -1  O  GLY A 106   N  ALA A  86           
SHEET    1 AA4 4 ILE A 121  ILE A 124  0                                        
SHEET    2 AA4 4 MET A 130  TYR A 136 -1  O  GLY A 132   N  ILE A 123           
SHEET    3 AA4 4 LEU A 139  PRO A 144 -1  O  LYS A 141   N  LEU A 133           
SHEET    4 AA4 4 PHE A 155  ARG A 158 -1  O  ILE A 157   N  PHE A 140           
SHEET    1 AA5 4 VAL A 164  PHE A 169  0                                        
SHEET    2 AA5 4 THR A 177  ASP A 184 -1  O  VAL A 181   N  ILE A 165           
SHEET    3 AA5 4 GLY A 187  SER A 196 -1  O  LYS A 191   N  PHE A 180           
SHEET    4 AA5 4 GLU A 201  LYS A 204 -1  O  GLU A 201   N  SER A 196           
SHEET    1 AA6 4 VAL A 164  PHE A 169  0                                        
SHEET    2 AA6 4 THR A 177  ASP A 184 -1  O  VAL A 181   N  ILE A 165           
SHEET    3 AA6 4 GLY A 187  SER A 196 -1  O  LYS A 191   N  PHE A 180           
SHEET    4 AA6 4 GLU A 210  ASN A 211 -1  O  GLU A 210   N  VAL A 190           
SHEET    1 AA7 4 MET A 218  ALA A 221  0                                        
SHEET    2 AA7 4 ALA A 229  ILE A 232 -1  O  ILE A 232   N  MET A 218           
SHEET    3 AA7 4 ILE A 237  ASN A 241 -1  O  THR A 238   N  ILE A 231           
SHEET    4 AA7 4 LYS A 244  ILE A 248 -1  O  LEU A 246   N  TYR A 239           
SHEET    1 AA8 4 ILE A 258  ARG A 263  0                                        
SHEET    2 AA8 4 ARG A 270  ASP A 275 -1  O  GLY A 274   N  VAL A 259           
SHEET    3 AA8 4 ARG A 279  GLU A 286 -1  O  PHE A 281   N  LEU A 273           
SHEET    4 AA8 4 ASP A 299  GLU A 307 -1  O  GLU A 303   N  MET A 282           
SHEET    1 AA9 4 CYS A 313  TYR A 316  0                                        
SHEET    2 AA9 4 VAL A 321  GLY A 325 -1  O  PHE A 323   N  THR A 315           
SHEET    3 AA9 4 SER A 331  LEU A 336 -1  O  VAL A 334   N  VAL A 322           
SHEET    4 AA9 4 VAL A 347  PHE A 353 -1  O  VAL A 348   N  LYS A 335           
SHEET    1 AB1 4 ASP A 361  VAL A 365  0                                        
SHEET    2 AB1 4 GLN A 374  SER A 379 -1  O  CYS A 378   N  ASP A 361           
SHEET    3 AB1 4 SER A 386  ARG A 391 -1  O  SER A 386   N  SER A 379           
SHEET    4 AB1 4 HIS A 711  PRO A 716 -1  O  VAL A 715   N  LEU A 387           
SHEET    1 AB2 3 SER A 720  GLN A 727  0                                        
SHEET    2 AB2 3 CYS A 732  GLN A 743 -1  O  LEU A 736   N  ARG A 722           
SHEET    3 AB2 3 THR A 749  ALA A 751 -1  O  THR A 750   N  VAL A 742           
SHEET    1 AB3 5 SER A 720  GLN A 727  0                                        
SHEET    2 AB3 5 CYS A 732  GLN A 743 -1  O  LEU A 736   N  ARG A 722           
SHEET    3 AB3 5 GLU A 785  ASP A 795 -1  O  LEU A 792   N  VAL A 735           
SHEET    4 AB3 5 VAL A 801  GLN A 806 -1  O  HIS A 805   N  LEU A 791           
SHEET    5 AB3 5 SER A 762  VAL A 765  1  N  SER A 764   O  GLN A 806           
SHEET    1 AB4 4 GLU A 811  CYS A 819  0                                        
SHEET    2 AB4 4 TYR A 828  MET A 835 -1  O  ILE A 830   N  VAL A 817           
SHEET    3 AB4 4 GLY A 846  SER A 854 -1  O  PHE A 851   N  PHE A 829           
SHEET    4 AB4 4 LYS A 857  VAL A 866 -1  O  ALA A 862   N  VAL A 850           
SHEET    1 AB5 4 VAL A 870  PHE A 876  0                                        
SHEET    2 AB5 4 LYS A 879  ILE A 884 -1  O  LEU A 881   N  VAL A 874           
SHEET    3 AB5 4 THR A 887  TRP A 893 -1  O  ARG A 889   N  ALA A 882           
SHEET    4 AB5 4 LEU A 899  TYR A 906 -1  O  GLU A 902   N  LEU A 890           
SHEET    1 AB6 4 TYR A 913  LYS A 917  0                                        
SHEET    2 AB6 4 PHE A 920  GLY A 924 -1  O  LEU A 922   N  LYS A 915           
SHEET    3 AB6 4 SER A 929  LYS A 936 -1  O  LEU A 931   N  VAL A 923           
SHEET    4 AB6 4 ASN A 941  PHE A 949 -1  O  ALA A 946   N  LEU A 932           
SHEET    1 AB7 4 ALA A 956  ILE A 959  0                                        
SHEET    2 AB7 4 ASN A 964  GLU A 969 -1  O  ALA A 968   N  ALA A 956           
SHEET    3 AB7 4 ASN A 973  GLN A 978 -1  O  PHE A 975   N  GLY A 967           
SHEET    4 AB7 4 GLN A 993  HIS A 999 -1  O  PHE A 998   N  LEU A 974           
SHEET    1 AB8 2 PHE A1076  THR A1078  0                                        
SHEET    2 AB8 2 LYS A1081  GLU A1083 -1  O  LYS A1081   N  THR A1078           
SHEET    1 AB9 7 GLU B  65  GLU B  66  0                                        
SHEET    2 AB9 7 GLU B 132  GLU B 147 -1  O  TYR B 144   N  GLU B  65           
SHEET    3 AB9 7 THR B 119  ASN B 127 -1  N  ALA B 124   O  PHE B 135           
SHEET    4 AB9 7 CYS B  78  VAL B  83  1  N  PRO B  82   O  ALA B 121           
SHEET    5 AB9 7 GLN B 178  ILE B 184 -1  O  ALA B 180   N  ILE B  81           
SHEET    6 AB9 7 ILE B 154  THR B 172 -1  N  ARG B 171   O  GLN B 179           
SHEET    7 AB9 7 THR B  96  LEU B 101 -1  N  LEU B 101   O  VAL B 155           
SHEET    1 AC1 4 GLU B  65  GLU B  66  0                                        
SHEET    2 AC1 4 GLU B 132  GLU B 147 -1  O  TYR B 144   N  GLU B  65           
SHEET    3 AC1 4 ILE B 154  THR B 172 -1  O  ARG B 162   N  THR B 138           
SHEET    4 AC1 4 THR B  96  LEU B 101 -1  N  LEU B 101   O  VAL B 155           
SHEET    1 AC2 3 GLU B 330  THR B 333  0                                        
SHEET    2 AC2 3 SER B 320  CYS B 323 -1  N  LEU B 321   O  THR B 332           
SHEET    3 AC2 3 LEU B 422  THR B 425 -1  O  LEU B 423   N  CYS B 322           
SHEET    1 AC3 6 MET B 346  VAL B 350  0                                        
SHEET    2 AC3 6 VAL B 356  VAL B 362 -1  O  HIS B 357   N  TYR B 349           
SHEET    3 AC3 6 LYS B 413  THR B 418 -1  O  TRP B 415   N  VAL B 362           
SHEET    4 AC3 6 HIS B 397  ALA B 404 -1  N  TRP B 400   O  GLY B 416           
SHEET    5 AC3 6 TYR B 384  CYS B 391 -1  N  ALA B 385   O  THR B 403           
SHEET    6 AC3 6 LEU B 368  SER B 375 -1  N  ILE B 371   O  VAL B 388           
LINK         SG  CYS B 323                ZN    ZN B 501     1555   1555  2.31  
LINK         SG  CYS B 326                ZN    ZN B 501     1555   1555  2.35  
LINK         SG  CYS B 391                ZN    ZN B 501     1555   1555  2.40  
LINK         SG  CYS B 394                ZN    ZN B 501     1555   1555  2.27  
CISPEP   1 GLU A  224    PRO A  225          0         3.71                     
CISPEP   2 GLY A  357    PRO A  358          0        -4.49                     
CISPEP   3 SER B  410    PRO B  411          0         0.96                     
SITE     1 AC1  4 CYS B 323  CYS B 326  CYS B 391  CYS B 394                    
SITE     1 AC2 16 ASN B 351  PRO B 352  HIS B 353  TYR B 355                    
SITE     2 AC2 16 HIS B 378  SER B 379  TRP B 380  TRP B 386                    
SITE     3 AC2 16 TRP B 400  PHE B 402  TRP C  81  PRO C  82                    
SITE     4 AC2 16 PHE C  83  LEU C  94  ASN C 140  ILE C 146                    
CRYST1  115.406  115.406  588.143  90.00  90.00 120.00 P 65 2 2     12          
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      0.008665  0.005003  0.000000        0.00000                         
SCALE2      0.000000  0.010006  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001700        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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