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Database: PDB
Entry: 3WIX
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HEADER    APOPTOSIS                               26-SEP-13   3WIX              
TITLE     CRYSTAL STRUCTURE OF MCL-1 IN COMPLEX WITH COMPOUND 4                 
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 FRAGMENT: UNP RESIDUES 172-327;                                      
COMPND   6 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN       
COMPND   7 EAT/MCL1, MCL1/EAT;                                                  
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1                                   
KEYWDS    REGULATION, APOPTOSIS                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SOGABE,S.IGAKI,Y.HAYANO                                             
REVDAT   2   12-MAR-14 3WIX    1       JRNL                                     
REVDAT   1   27-NOV-13 3WIX    0                                                
JRNL        AUTH   Y.TANAKA,K.AIKAWA,G.NISHIDA,M.HOMMA,S.SOGABE,S.IGAKI,        
JRNL        AUTH 2 Y.HAYANO,T.SAMESHIMA,I.MIYAHISA,T.KAWAMOTO,M.TAWADA,Y.IMAI,  
JRNL        AUTH 3 M.INAZUKA,N.CHO,Y.IMAEDA,T.ISHIKAWA                          
JRNL        TITL   DISCOVERY OF POTENT MCL-1/BCL-XL DUAL INHIBITORS BY USING A  
JRNL        TITL 2 HYBRIDIZATION STRATEGY BASED ON STRUCTURAL ANALYSIS OF       
JRNL        TITL 3 TARGET PROTEINS.                                             
JRNL        REF    J.MED.CHEM.                   V.  56  9635 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24215352                                                     
JRNL        DOI    10.1021/JM401170C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 39802                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2128                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2954                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4735                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.59000                                              
REMARK   3    B22 (A**2) : -1.33000                                             
REMARK   3    B33 (A**2) : -2.27000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.25000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.241         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.554        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4967 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6688 ; 1.428 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   581 ; 5.268 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   238 ;38.901 ;22.773       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   901 ;17.879 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;17.636 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   724 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3950 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2342 ; 3.557 ; 2.555       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2917 ; 4.625 ; 4.281       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2625 ; 4.736 ; 2.986       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  7905 ; 7.444 ;12.053       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   172        A   321                          
REMARK   3    RESIDUE RANGE :   A   501        A   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1312   0.0151 -49.1875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0288 T22:   0.1259                                     
REMARK   3      T33:   0.1071 T12:  -0.0110                                     
REMARK   3      T13:   0.0203 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7717 L22:   2.9771                                     
REMARK   3      L33:   2.6625 L12:   0.0736                                     
REMARK   3      L13:   0.3031 L23:  -0.4304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1133 S12:   0.0112 S13:   0.0084                       
REMARK   3      S21:  -0.0449 S22:  -0.0288 S23:  -0.0912                       
REMARK   3      S31:   0.1629 S32:   0.0719 S33:  -0.0845                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   172        B   321                          
REMARK   3    RESIDUE RANGE :   B   501        B   501                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1611  -1.5995 -20.0747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0482 T22:   0.2198                                     
REMARK   3      T33:   0.1603 T12:   0.0138                                     
REMARK   3      T13:  -0.0109 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8523 L22:   3.7491                                     
REMARK   3      L33:   3.9276 L12:   0.5100                                     
REMARK   3      L13:  -0.3847 L23:   0.3118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0641 S12:   0.0022 S13:   0.0147                       
REMARK   3      S21:  -0.2757 S22:  -0.0105 S23:   0.1723                       
REMARK   3      S31:  -0.3109 S32:  -0.2614 S33:  -0.0536                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   172        C   321                          
REMARK   3    RESIDUE RANGE :   C   501        C   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0812 -29.3686 -28.6838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0242 T22:   0.1400                                     
REMARK   3      T33:   0.1696 T12:  -0.0038                                     
REMARK   3      T13:   0.0179 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6333 L22:   2.0630                                     
REMARK   3      L33:   2.8522 L12:   0.5024                                     
REMARK   3      L13:   0.4238 L23:  -0.4456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:  -0.1301 S13:  -0.1836                       
REMARK   3      S21:  -0.1683 S22:   0.0122 S23:  -0.0826                       
REMARK   3      S31:   0.1962 S32:   0.0566 S33:   0.0057                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   172        D   321                          
REMARK   3    RESIDUE RANGE :   D   501        D   501                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1450  27.6896   1.0058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0995 T22:   0.0944                                     
REMARK   3      T33:   0.1213 T12:  -0.0190                                     
REMARK   3      T13:   0.0018 T23:   0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6134 L22:   3.0859                                     
REMARK   3      L33:   3.1233 L12:   0.7492                                     
REMARK   3      L13:  -0.0947 L23:  -0.1405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0504 S12:   0.0852 S13:   0.2044                       
REMARK   3      S21:  -0.0717 S22:   0.0818 S23:   0.1388                       
REMARK   3      S31:  -0.1677 S32:  -0.0514 S33:  -0.0313                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3WIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096392.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41960                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2PQK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.0, 0.2M SODIUM            
REMARK 280  ISOTHIOCYANATE, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
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       66.91450            
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     GLY A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     LEU A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     SER 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     GLY B   167                                                      
REMARK 465     PRO B   168                                                      
REMARK 465     LEU B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
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     GLY C   167                                                      
REMARK 465     PRO C   168                                                      
REMARK 465     LEU C   169                                                      
REMARK 465     GLY C   170                                                      
REMARK 465     SER C   171                                                      
REMARK 465     LYS C   197                                                      
REMARK 465     PRO C   198                                                      
REMARK 465     MET C   199                                                      
REMARK 465     GLY C   200                                                      
REMARK 465     ARG C   201                                                      
REMARK 465     SER C   202                                                      
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     GLY D   167                                                      
REMARK 465     PRO D   168                                                      
REMARK 465     LEU D   169                                                      
REMARK 465     GLY D   170                                                      
REMARK 465     SER D   171                                                      
REMARK 465     THR D   196                                                      
REMARK 465     LYS D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     MET D   199                                                      
REMARK 465     GLY D   200                                                      
REMARK 465     ARG D   201                                                      
REMARK 465     SER D   202                                                      
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 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 236       76.10     45.63                                   
REMARK 500    PHE B 319       54.94   -102.01                                   
REMARK 500    ASP C 236       65.86     39.03                                   
REMARK 500    SER C 247      -39.06    -36.86                                   
REMARK 500    LEU D 298      -70.80    -49.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 912        DISTANCE =  5.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC3 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC3 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC3 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC3 D 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WIY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WIZ   RELATED DB: PDB                                   
DBREF  3WIX A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIX B  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIX C  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIX D  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
SEQADV 3WIX GLY A  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX PRO A  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX LEU A  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY B  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX PRO B  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX LEU B  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX SER B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY C  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX PRO C  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX LEU C  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX SER C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY D  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX PRO D  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX LEU D  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX GLY D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIX SER D  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 A  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 A  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 A  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 A  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 A  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 A  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 A  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 A  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 A  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 A  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 A  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 A  161  ASP LEU GLU GLY GLY                                          
SEQRES   1 B  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 B  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 B  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 B  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 B  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 B  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 B  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 B  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 B  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 B  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 B  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 B  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 B  161  ASP LEU GLU GLY GLY                                          
SEQRES   1 C  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 C  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 C  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 C  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 C  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 C  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 C  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 C  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 C  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 C  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 C  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 C  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 C  161  ASP LEU GLU GLY GLY                                          
SEQRES   1 D  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 D  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 D  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 D  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 D  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 D  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 D  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 D  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 D  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 D  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 D  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 D  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 D  161  ASP LEU GLU GLY GLY                                          
HET    LC3  A 501      35                                                       
HET    LC3  B 501      35                                                       
HET    LC3  C 501      35                                                       
HET    LC3  D 501      35                                                       
HETNAM     LC3 7-(4-CARBOXYPHENYL)-3-[3-(NAPHTHALEN-1-YLOXY)                    
HETNAM   2 LC3  PROPYL]PYRAZOLO[1,5-A]PYRIDINE-2-CARBOXYLIC ACID                
FORMUL   5  LC3    4(C28 H22 N2 O5)                                             
FORMUL   9  HOH   *79(H2 O)                                                     
HELIX    1   1 ASP A  172  GLY A  192  1                                  21    
HELIX    2   2 GLY A  203  HIS A  224  1                                  22    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 ASN A  239  LYS A  244  1                                   6    
HELIX    5   5 LEU A  246  SER A  255  1                                  10    
HELIX    6   6 ASN A  260  ILE A  281  1                                  22    
HELIX    7   7 GLN A  283  SER A  285  5                                   3    
HELIX    8   8 CYS A  286  GLN A  309  1                                  24    
HELIX    9   9 ARG A  310  PHE A  319  1                                  10    
HELIX   10  10 GLU B  173  GLY B  192  1                                  20    
HELIX   11  11 GLY B  203  HIS B  224  1                                  22    
HELIX   12  12 HIS B  224  ASP B  236  1                                  13    
HELIX   13  13 ASN B  239  SER B  245  1                                   7    
HELIX   14  14 LEU B  246  SER B  255  1                                  10    
HELIX   15  15 ASN B  260  ILE B  281  1                                  22    
HELIX   16  16 GLN B  283  SER B  285  5                                   3    
HELIX   17  17 CYS B  286  GLN B  309  1                                  24    
HELIX   18  18 ARG B  310  PHE B  319  1                                  10    
HELIX   19  19 GLU C  173  GLY C  192  1                                  20    
HELIX   20  20 ALA C  204  HIS C  224  1                                  21    
HELIX   21  21 HIS C  224  ASP C  236  1                                  13    
HELIX   22  22 ASN C  239  SER C  245  1                                   7    
HELIX   23  23 LEU C  246  SER C  255  1                                  10    
HELIX   24  24 ASN C  260  ILE C  281  1                                  22    
HELIX   25  25 GLN C  283  SER C  285  5                                   3    
HELIX   26  26 CYS C  286  GLN C  309  1                                  24    
HELIX   27  27 ARG C  310  HIS C  320  1                                  11    
HELIX   28  28 GLU D  173  GLY D  192  1                                  20    
HELIX   29  29 ALA D  204  HIS D  224  1                                  21    
HELIX   30  30 HIS D  224  ASP D  236  1                                  13    
HELIX   31  31 ASN D  239  ASP D  256  1                                  18    
HELIX   32  32 ASN D  260  ILE D  281  1                                  22    
HELIX   33  33 GLN D  283  SER D  285  5                                   3    
HELIX   34  34 CYS D  286  GLN D  309  1                                  24    
HELIX   35  35 ARG D  310  HIS D  320  1                                  11    
SITE     1 AC1  9 ALA A 227  MET A 250  VAL A 253  PHE A 254                    
SITE     2 AC1  9 ARG A 263  THR A 266  LEU A 267  PHE A 270                    
SITE     3 AC1  9 ILE A 294                                                     
SITE     1 AC2 10 ALA B 227  LEU B 235  MET B 250  VAL B 253                    
SITE     2 AC2 10 PHE B 254  ARG B 263  THR B 266  LEU B 267                    
SITE     3 AC2 10 PHE B 270  ILE B 294                                          
SITE     1 AC3 19 PRO A 198  MET A 199  ARG A 201  SER A 202                    
SITE     2 AC3 19 ARG A 207  HOH A 906  HOH A 908  HIS C 224                    
SITE     3 AC3 19 ALA C 227  PHE C 228  MET C 231  MET C 250                    
SITE     4 AC3 19 VAL C 253  ARG C 263  THR C 266  LEU C 267                    
SITE     5 AC3 19 PHE C 270  GLY C 271  HOH C 901                               
SITE     1 AC4 16 MET B 199  ARG B 201  SER B 202  ARG B 207                    
SITE     2 AC4 16 HOH B 906  ALA D 227  PHE D 228  MET D 231                    
SITE     3 AC4 16 MET D 250  VAL D 253  ARG D 263  THR D 266                    
SITE     4 AC4 16 LEU D 267  PHE D 270  GLY D 271  HOH D 902                    
CRYST1   38.169  133.829   58.243  90.00  89.94  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      0.026199  0.000000 -0.000026        0.00000                         
SCALE2      0.000000  0.007472  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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