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Database: PDB
Entry: 6BW2
LinkDB: 6BW2
Original site: 6BW2 
HEADER    APOPTOSIS                               14-DEC-17   6BW2              
TITLE     MCL-1 COMPLEXED WITH SMALL MOLECULES                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   6 EAT/MCL1,MCL1/EAT;                                                   
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MCL-1 INHIBITOR, CANCER, STRUCTURE-BASED DESIGN, DRUG DISCOVERY,      
KEYWDS   2 APOPTOSIS                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO                                                                
REVDAT   4   04-DEC-19 6BW2    1       REMARK                                   
REVDAT   3   04-APR-18 6BW2    1       JRNL                                     
REVDAT   2   21-MAR-18 6BW2    1       JRNL                                     
REVDAT   1   31-JAN-18 6BW2    0                                                
JRNL        AUTH   S.SHAW,Z.BIAN,B.ZHAO,J.C.TARR,N.VEERASAMY,K.O.JEON,J.BELMAR, 
JRNL        AUTH 2 A.L.ARNOLD,S.A.FOGARTY,E.PERRY,J.L.SENSINTAFFAR,D.V.CAMPER,  
JRNL        AUTH 3 O.W.ROSSANESE,T.LEE,E.T.OLEJNICZAK,S.W.FESIK                 
JRNL        TITL   OPTIMIZATION OF POTENT AND SELECTIVE TRICYCLIC INDOLE        
JRNL        TITL 2 DIAZEPINONE MYELOID CELL LEUKEMIA-1 INHIBITORS USING         
JRNL        TITL 3 STRUCTURE-BASED DESIGN.                                      
JRNL        REF    J. MED. CHEM.                 V.  61  2410 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29323899                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01155                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 3.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25203                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1207                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 26.1390 -  5.7032    0.95     2789   139  0.2591 0.2441        
REMARK   3     2  5.7032 -  4.5345    0.95     2758   145  0.2293 0.2615        
REMARK   3     3  4.5345 -  3.9636    0.95     2728   126  0.2185 0.2410        
REMARK   3     4  3.9636 -  3.6022    0.95     2731   125  0.2363 0.2864        
REMARK   3     5  3.6022 -  3.3446    0.94     2722   120  0.2435 0.2755        
REMARK   3     6  3.3446 -  3.1477    0.92     2659   136  0.2554 0.2743        
REMARK   3     7  3.1477 -  2.9903    0.90     2550   126  0.2647 0.2439        
REMARK   3     8  2.9903 -  2.8603    0.87     2549   141  0.2703 0.2821        
REMARK   3     9  2.8603 -  2.7503    0.87     2501   139  0.2829 0.3334        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.240           
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      :  0.003           4995                                  
REMARK   3   ANGLE     :  0.694           6767                                  
REMARK   3   CHIRALITY :  0.037            722                                  
REMARK   3   PLANARITY :  0.003            851                                  
REMARK   3   DIHEDRAL  : 11.658           2862                                  
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):  50.5270 -33.2684  22.2962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7039 T22:   0.6525                                     
REMARK   3      T33:   0.4228 T12:   0.0487                                     
REMARK   3      T13:  -0.0047 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2497 L22:   0.2822                                     
REMARK   3      L33:   0.1603 L12:  -0.0232                                     
REMARK   3      L13:   0.0116 L23:   0.0551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:   0.0136 S13:  -0.0680                       
REMARK   3      S21:  -0.0961 S22:  -0.0561 S23:   0.0121                       
REMARK   3      S31:   0.0576 S32:   0.0279 S33:   0.0000                       
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 6BW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231685.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-15                          
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                       : 21-ID-F                            
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25203                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.71900                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 4ZBF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%-30% PEG 3350, MAGNESIUM CHLORIDE,    
REMARK 280  BIS-TRIS, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       67.18450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     ALA A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     ASP B   172                                                      
REMARK 465     VAL B   321                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     ALA C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     VAL C   321                                                      
REMARK 465     GLU C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     LEU C   324                                                      
REMARK 465     GLU C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     ALA D   170                                                      
REMARK 465     ASP D   171                                                      
REMARK 465     ASP D   172                                                      
REMARK 465     VAL D   321                                                      
REMARK 465     GLU D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     LEU D   324                                                      
REMARK 465     GLU D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     GLY D   327                                                      
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 180    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     PRO A 198    CG   CD                                             
REMARK 470     MET A 199    CG   SD   CE                                        
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 226    OG1  CG2                                            
REMARK 470     LYS A 279    NZ                                                  
REMARK 470     LYS A 308    CE   NZ                                             
REMARK 470     GLU B 180    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     PRO B 198    CG   CD                                             
REMARK 470     MET B 199    CG   SD   CE                                        
REMARK 470     SER B 202    OG                                                  
REMARK 470     LYS B 234    CD   CE   NZ                                        
REMARK 470     ILE B 237    CG1  CG2  CD1                                       
REMARK 470     LYS B 244    CE   NZ                                             
REMARK 470     ASP C 172    CG   OD1  OD2                                       
REMARK 470     ARG C 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 197    CG   CD   CE   NZ                                   
REMARK 470     MET C 199    SD   CE                                             
REMARK 470     GLU C 211    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 220    CG1  CG2                                            
REMARK 470     ARG C 222    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 244    CE   NZ                                             
REMARK 470     ILE C 251    CD1                                                 
REMARK 470     LYS C 308    CG   CD   CE   NZ                                   
REMARK 470     ARG C 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 173    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 177    CG   CD   OE1  NE2                                  
REMARK 470     ILE D 181    CG1  CG2  CD1                                       
REMARK 470     ASP D 195    OD2                                                 
REMARK 470     MET D 199    SD   CE                                             
REMARK 470     SER D 202    OG                                                  
REMARK 470     LEU D 210    CD1  CD2                                            
REMARK 470     LYS D 244    CD   CE   NZ                                        
REMARK 470     VAL D 258    CG1  CG2                                            
REMARK 470     LYS D 279    CG   CD   CE   NZ                                   
REMARK 470     ARG D 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 317    CG   CD   OE1  OE2                                  
REMARK 470     PHE D 319    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 195      131.93     44.77                                   
REMARK 500    THR A 196     -133.92    -80.01                                   
REMARK 500    LYS A 197      153.02     65.66                                   
REMARK 500    MET A 199       44.93    -88.60                                   
REMARK 500    LYS A 238      -40.46   -133.17                                   
REMARK 500    PHE A 319       48.09   -101.41                                   
REMARK 500    ASP B 195      105.16     62.24                                   
REMARK 500    ASN B 239     -166.58   -162.07                                   
REMARK 500    PHE B 319       45.78   -100.80                                   
REMARK 500    GLU C 173      -38.77   -141.16                                   
REMARK 500    ASP C 195      109.76    -47.53                                   
REMARK 500    THR C 196     -125.03    -74.00                                   
REMARK 500    LYS C 197      152.89     67.16                                   
REMARK 500    ASP C 236       70.01     50.08                                   
REMARK 500    PHE C 319       48.77   -102.41                                   
REMARK 500    ASP D 195      110.14     33.37                                   
REMARK 500    THR D 196     -138.65    -74.32                                   
REMARK 500    LYS D 197      150.17     60.59                                   
REMARK 500    GLN D 283       56.57   -140.36                                   
REMARK 500    PHE D 319       44.59   -106.14                                   
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 ECY A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ECY B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ECY C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ECY D 400                 
DBREF  6BW2 A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  6BW2 B  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  6BW2 C  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  6BW2 D  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
SEQADV 6BW2 ALA A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ASP A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ALA B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ASP B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ALA C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ASP C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ALA D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 6BW2 ASP D  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  158  ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 A  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 A  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 A  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 A  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 A  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 A  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 A  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 A  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 A  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 A  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 A  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 A  158  GLY GLY                                                      
SEQRES   1 B  158  ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 B  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 B  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 B  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 B  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 B  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 B  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 B  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 B  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 B  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 B  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 B  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 B  158  GLY GLY                                                      
SEQRES   1 C  158  ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 C  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 C  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 C  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 C  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 C  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 C  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 C  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 C  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 C  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 C  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 C  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 C  158  GLY GLY                                                      
SEQRES   1 D  158  ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 D  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 D  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 D  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 D  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 D  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 D  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 D  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 D  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 D  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 D  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 D  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 D  158  GLY GLY                                                      
HET    ECY  A 400      46                                                       
HET    ECY  B 400      46                                                       
HET    ECY  C 400      46                                                       
HET    ECY  D 400      46                                                       
HETNAM     ECY 3-({11-[3-(4-CHLORO-3,5-DIMETHYLPHENOXY)PROPYL]-1-OXO-           
HETNAM   2 ECY  7-(1,3,5-TRIMETHYL-1H-PYRAZOL-4-YL)-4,5-DIHYDRO-1H-[1,          
HETNAM   3 ECY  4]DIAZEPINO[1,2-A]INDOL-2(3H)-YL}METHYL)BENZOIC ACID            
FORMUL   5  ECY    4(C37 H39 CL N4 O4)                                          
FORMUL   9  HOH   *24(H2 O)                                                     
HELIX    1 AA1 GLU A  173  GLY A  192  1                                  20    
HELIX    2 AA2 SER A  202  HIS A  224  1                                  23    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  ASP A  256  1                                  18    
HELIX    5 AA5 ASN A  260  ILE A  281  1                                  22    
HELIX    6 AA6 GLN A  283  SER A  285  5                                   3    
HELIX    7 AA7 CYS A  286  GLN A  309  1                                  24    
HELIX    8 AA8 GLY A  311  PHE A  319  1                                   9    
HELIX    9 AA9 LEU B  174  GLY B  192  1                                  19    
HELIX   10 AB1 SER B  202  HIS B  224  1                                  23    
HELIX   11 AB2 HIS B  224  ASP B  236  1                                  13    
HELIX   12 AB3 ASN B  239  LYS B  244  1                                   6    
HELIX   13 AB4 LEU B  246  ASP B  256  1                                  11    
HELIX   14 AB5 ASN B  260  ILE B  281  1                                  22    
HELIX   15 AB6 GLN B  283  SER B  285  5                                   3    
HELIX   16 AB7 CYS B  286  GLN B  309  1                                  24    
HELIX   17 AB8 ARG B  310  PHE B  319  1                                  10    
HELIX   18 AB9 GLU C  173  GLY C  192  1                                  20    
HELIX   19 AC1 SER C  202  HIS C  224  1                                  23    
HELIX   20 AC2 HIS C  224  ASP C  236  1                                  13    
HELIX   21 AC3 ASN C  239  LYS C  244  1                                   6    
HELIX   22 AC4 LEU C  246  ASP C  256  1                                  11    
HELIX   23 AC5 ASN C  260  ILE C  281  1                                  22    
HELIX   24 AC6 GLN C  283  SER C  285  5                                   3    
HELIX   25 AC7 CYS C  286  GLN C  309  1                                  24    
HELIX   26 AC8 ARG C  310  PHE C  319  1                                  10    
HELIX   27 AC9 LEU D  174  GLY D  192  1                                  19    
HELIX   28 AD1 SER D  202  HIS D  224  1                                  23    
HELIX   29 AD2 HIS D  224  ASP D  236  1                                  13    
HELIX   30 AD3 ASN D  239  LYS D  244  1                                   6    
HELIX   31 AD4 LEU D  246  ASP D  256  1                                  11    
HELIX   32 AD5 ASN D  260  ILE D  281  1                                  22    
HELIX   33 AD6 GLN D  283  SER D  285  5                                   3    
HELIX   34 AD7 CYS D  286  GLN D  309  1                                  24    
HELIX   35 AD8 ARG D  310  PHE D  319  1                                  10    
SITE     1 AC1 10 HIS A 224  ALA A 227  PHE A 228  LEU A 246                    
SITE     2 AC1 10 MET A 250  VAL A 253  ARG A 263  LEU A 267                    
SITE     3 AC1 10 PHE A 270  GLY A 271                                          
SITE     1 AC2 11 ALA B 227  PHE B 228  LEU B 246  MET B 250                    
SITE     2 AC2 11 ASN B 260  GLY B 262  ARG B 263  THR B 266                    
SITE     3 AC2 11 LEU B 267  PHE B 270  GLY B 271                               
SITE     1 AC3 12 HIS B 252  HIS C 224  ALA C 227  PHE C 228                    
SITE     2 AC3 12 LEU C 246  MET C 250  ASN C 260  GLY C 262                    
SITE     3 AC3 12 ARG C 263  THR C 266  LEU C 267  PHE C 270                    
SITE     1 AC4 13 ALA D 227  PHE D 228  LEU D 246  MET D 250                    
SITE     2 AC4 13 VAL D 253  PHE D 254  GLY D 262  ARG D 263                    
SITE     3 AC4 13 THR D 266  LEU D 267  PHE D 270  GLY D 271                    
SITE     4 AC4 13 ILE D 294                                                     
CRYST1   39.284  134.369   96.561  90.00  90.04  90.00 P 1 21 1      8          
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      0.025456  0.000000  0.000016        0.00000                         
SCALE2      0.000000  0.007442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010356        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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