GenomeNet

Database: PDB
Entry: 3WIY
LinkDB: 3WIY
Original site: 3WIY 
HEADER    APOPTOSIS                               26-SEP-13   3WIY              
TITLE     CRYSTAL STRUCTURE OF MCL-1 IN COMPLEX WITH COMPOUND 10                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B, C, D, E, F;                                             
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 3WIY    1       JRNL                                     
REVDAT   1   27-NOV-13 3WIY    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.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43840                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2335                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3263                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 187                          
REMARK   3   BIN FREE R VALUE                    : 0.3680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7291                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 378                                     
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.26000                                             
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : -0.08000                                             
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.15000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.369         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.266         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.208         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.252        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7825 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10552 ; 1.443 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   899 ; 5.037 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   365 ;36.724 ;22.767       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1394 ;17.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;20.289 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1115 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6412 ; 0.005 ; 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):  3614 ; 5.263 ; 3.777       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4507 ; 6.727 ; 6.331       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4211 ; 7.534 ; 4.347       
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): 12515 ;10.843 ;17.283       
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  : 6                                          
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   323                          
REMARK   3    RESIDUE RANGE :   A   501        A   501                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.6155  -4.6377  29.9402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1022 T22:   0.0350                                     
REMARK   3      T33:   0.0383 T12:  -0.0179                                     
REMARK   3      T13:  -0.0322 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4592 L22:   1.0535                                     
REMARK   3      L33:   0.7402 L12:   0.5301                                     
REMARK   3      L13:   0.2402 L23:   0.4176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:   0.0298 S13:  -0.0594                       
REMARK   3      S21:   0.1147 S22:   0.0292 S23:  -0.0572                       
REMARK   3      S31:   0.0654 S32:  -0.0405 S33:  -0.0599                       
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   322                          
REMARK   3    RESIDUE RANGE :   B   501        B   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1849   0.3502  -0.0090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0533 T22:   0.1395                                     
REMARK   3      T33:   0.0411 T12:   0.0223                                     
REMARK   3      T13:  -0.0272 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3295 L22:   1.1209                                     
REMARK   3      L33:   0.6992 L12:  -0.5461                                     
REMARK   3      L13:   0.1239 L23:   0.0533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0436 S12:   0.0649 S13:  -0.0122                       
REMARK   3      S21:   0.0179 S22:   0.0277 S23:  -0.0237                       
REMARK   3      S31:   0.0783 S32:   0.0404 S33:  -0.0713                       
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): -19.6772  39.2050 -41.6054              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0737 T22:   0.0781                                     
REMARK   3      T33:   0.0679 T12:  -0.0005                                     
REMARK   3      T13:   0.0304 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3486 L22:   0.7705                                     
REMARK   3      L33:   0.6997 L12:  -0.3875                                     
REMARK   3      L13:  -0.3028 L23:  -0.0180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0186 S12:   0.0093 S13:   0.0152                       
REMARK   3      S21:   0.0410 S22:   0.0509 S23:   0.0567                       
REMARK   3      S31:  -0.0612 S32:   0.0024 S33:  -0.0695                       
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):   6.0561  27.5063  21.8335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0548 T22:   0.0633                                     
REMARK   3      T33:   0.0682 T12:  -0.0334                                     
REMARK   3      T13:   0.0196 T23:  -0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3472 L22:   0.6102                                     
REMARK   3      L33:   0.6983 L12:  -0.1206                                     
REMARK   3      L13:  -0.2510 L23:   0.1784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0735 S12:  -0.0877 S13:   0.0888                       
REMARK   3      S21:  -0.0728 S22:   0.0122 S23:   0.0042                       
REMARK   3      S31:   0.0121 S32:   0.0011 S33:  -0.0856                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   172        E   323                          
REMARK   3    RESIDUE RANGE :   E   501        E   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9570  31.7101 -12.3724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0987 T22:   0.0849                                     
REMARK   3      T33:   0.0264 T12:  -0.0278                                     
REMARK   3      T13:   0.0340 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3430 L22:   1.7270                                     
REMARK   3      L33:   0.4760 L12:   0.3414                                     
REMARK   3      L13:  -0.2261 L23:  -0.4850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1461 S12:  -0.0877 S13:   0.0520                       
REMARK   3      S21:   0.1026 S22:  -0.0773 S23:   0.0514                       
REMARK   3      S31:  -0.0419 S32:   0.1022 S33:  -0.0688                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   172        F   321                          
REMARK   3    RESIDUE RANGE :   F   501        F   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7442   5.2755 -32.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0347 T22:   0.0839                                     
REMARK   3      T33:   0.0901 T12:  -0.0032                                     
REMARK   3      T13:  -0.0142 T23:   0.0743                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6053 L22:   0.5295                                     
REMARK   3      L33:   0.8160 L12:  -0.2338                                     
REMARK   3      L13:  -0.0483 L23:  -0.0622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0151 S12:  -0.0959 S13:  -0.1742                       
REMARK   3      S21:  -0.1157 S22:  -0.0273 S23:   0.0659                       
REMARK   3      S31:  -0.0400 S32:   0.0836 S33:   0.0122                       
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 3WIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096393.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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-NW12A                           
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 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46298                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
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     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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   (%): 41.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 22% PEG 3350,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: E                                     
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: 6                                                       
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: F                                     
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     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     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     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     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 465     GLY E   167                                                      
REMARK 465     PRO E   168                                                      
REMARK 465     LEU E   169                                                      
REMARK 465     GLY E   170                                                      
REMARK 465     SER E   171                                                      
REMARK 465     LEU E   324                                                      
REMARK 465     GLU E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLY E   327                                                      
REMARK 465     GLY F   167                                                      
REMARK 465     PRO F   168                                                      
REMARK 465     LEU F   169                                                      
REMARK 465     GLY F   170                                                      
REMARK 465     SER F   171                                                      
REMARK 465     GLU F   322                                                      
REMARK 465     ASP F   323                                                      
REMARK 465     LEU F   324                                                      
REMARK 465     GLU F   325                                                      
REMARK 465     GLY F   326                                                      
REMARK 465     GLY F   327                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS E   244     O    HOH E   405              2.02            
REMARK 500   NH1  ARG C   248     O    HOH C   928              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A 199     -120.53    -78.23                                   
REMARK 500    SER A 202       60.56   -117.06                                   
REMARK 500    SER B 202       32.26    -94.41                                   
REMARK 500    VAL B 321     -139.24   -134.27                                   
REMARK 500    LYS C 197      139.35    -35.68                                   
REMARK 500    MET C 199     -178.22    -67.04                                   
REMARK 500    ARG C 201      -84.45    -28.79                                   
REMARK 500    SER D 202       34.97    -76.04                                   
REMARK 500    ASN E 239     -172.31   -178.33                                   
REMARK 500    HIS E 320      106.39    -58.61                                   
REMARK 500    ARG F 201      -74.47    -79.96                                   
REMARK 500    ARG F 215      -74.67    -60.64                                   
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 LC6 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC6 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC6 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC6 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC6 E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC6 F 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WIX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WIZ   RELATED DB: PDB                                   
DBREF  3WIY A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIY B  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIY C  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIY D  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIY E  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3WIY F  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
SEQADV 3WIY GLY A  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO A  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU A  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY B  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO B  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU B  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY C  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO C  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU C  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY D  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO D  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU D  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER D  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY E  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO E  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU E  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY E  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER E  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY F  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY PRO F  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY LEU F  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY GLY F  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3WIY SER F  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                                          
SEQRES   1 E  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 E  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 E  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 E  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 E  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 E  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 E  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 E  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 E  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 E  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 E  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 E  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 E  161  ASP LEU GLU GLY GLY                                          
SEQRES   1 F  161  GLY PRO LEU GLY SER ASP GLU LEU TYR ARG GLN SER LEU          
SEQRES   2 F  161  GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY          
SEQRES   3 F  161  ALA LYS ASP THR LYS PRO MET GLY ARG SER GLY ALA THR          
SEQRES   4 F  161  SER ARG LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP          
SEQRES   5 F  161  GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET          
SEQRES   6 F  161  LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS          
SEQRES   7 F  161  SER LEU SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY          
SEQRES   8 F  161  VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE          
SEQRES   9 F  161  GLY ALA PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN          
SEQRES  10 F  161  GLU SER CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP          
SEQRES  11 F  161  VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN          
SEQRES  12 F  161  ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU          
SEQRES  13 F  161  ASP LEU GLU GLY GLY                                          
HET    LC6  A 501      63                                                       
HET    LC6  B 501      63                                                       
HET    LC6  C 501      63                                                       
HET    LC6  D 501      63                                                       
HET    LC6  E 501      63                                                       
HET    LC6  F 501      63                                                       
HETNAM     LC6 7-(4-{[(4-{[(2R)-4-(DIMETHYLAMINO)-1-(PHENYLSULFANYL)            
HETNAM   2 LC6  BUTAN-2-YL]AMINO}-3-NITROPHENYL)SULFONYL]CARBAMOYL}-2-          
HETNAM   3 LC6  METHYLPHENYL)-3-[3-(NAPHTHALEN-1-YLOXY)                         
HETNAM   4 LC6  PROPYL]PYRAZOLO[1,5-A]PYRIDINE-2-CARBOXYLIC ACID                
FORMUL   7  LC6    6(C47 H46 N6 O8 S2)                                          
FORMUL  13  HOH   *138(H2 O)                                                    
HELIX    1   1 ASP A  172  GLY A  192  1                                  21    
HELIX    2   2 SER A  202  HIS A  224  1                                  23    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 ASN A  239  SER A  245  1                                   7    
HELIX    5   5 SER A  245  SER A  255  1                                  11    
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  HIS A  320  1                                  11    
HELIX   10  10 GLU B  173  GLY B  192  1                                  20    
HELIX   11  11 SER B  202  HIS B  224  1                                  23    
HELIX   12  12 HIS B  224  ASP B  236  1                                  13    
HELIX   13  13 ASN B  239  LYS B  244  1                                   6    
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  HIS B  320  1                                  11    
HELIX   19  19 GLU C  173  GLY C  192  1                                  20    
HELIX   20  20 SER C  202  HIS C  224  1                                  23    
HELIX   21  21 HIS C  224  ASP C  236  1                                  13    
HELIX   22  22 ASN C  239  LYS C  244  1                                   6    
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 SER D  202  HIS D  224  1                                  23    
HELIX   30  30 HIS D  224  ASP D  236  1                                  13    
HELIX   31  31 ASN D  239  LEU D  246  1                                   8    
HELIX   32  32 LEU D  246  SER D  255  1                                  10    
HELIX   33  33 ASN D  260  ILE D  281  1                                  22    
HELIX   34  34 GLN D  283  SER D  285  5                                   3    
HELIX   35  35 CYS D  286  GLN D  309  1                                  24    
HELIX   36  36 ARG D  310  PHE D  319  1                                  10    
HELIX   37  37 GLU E  173  GLY E  192  1                                  20    
HELIX   38  38 SER E  202  HIS E  224  1                                  23    
HELIX   39  39 HIS E  224  ASP E  236  1                                  13    
HELIX   40  40 ASN E  239  SER E  245  1                                   7    
HELIX   41  41 SER E  245  ASP E  256  1                                  12    
HELIX   42  42 ASN E  260  ILE E  281  1                                  22    
HELIX   43  43 GLN E  283  SER E  285  5                                   3    
HELIX   44  44 CYS E  286  GLN E  309  1                                  24    
HELIX   45  45 ARG E  310  HIS E  320  1                                  11    
HELIX   46  46 GLU F  173  GLY F  192  1                                  20    
HELIX   47  47 SER F  202  HIS F  224  1                                  23    
HELIX   48  48 HIS F  224  ASP F  236  1                                  13    
HELIX   49  49 ASN F  239  SER F  245  1                                   7    
HELIX   50  50 LEU F  246  ASP F  256  1                                  11    
HELIX   51  51 ASN F  260  ILE F  281  1                                  22    
HELIX   52  52 GLN F  283  SER F  285  5                                   3    
HELIX   53  53 CYS F  286  GLN F  309  1                                  24    
HELIX   54  54 ARG F  310  PHE F  319  1                                  10    
SITE     1 AC1 16 THR A 226  ALA A 227  PHE A 228  GLY A 230                    
SITE     2 AC1 16 LYS A 234  LEU A 246  MET A 250  VAL A 253                    
SITE     3 AC1 16 ARG A 263  THR A 266  LEU A 267  PHE A 270                    
SITE     4 AC1 16 GLU B 225  THR B 226  SER D 255  ARG D 300                    
SITE     1 AC2 10 HIS B 224  ALA B 227  PHE B 228  LEU B 235                    
SITE     2 AC2 10 VAL B 253  ARG B 263  THR B 266  LEU B 267                    
SITE     3 AC2 10 PHE B 270  LC6 D 501                                          
SITE     1 AC3 11 GLU A 322  HIS C 224  LEU C 235  MET C 250                    
SITE     2 AC3 11 VAL C 253  ARG C 263  LEU C 267  PHE C 270                    
SITE     3 AC3 11 HOH C 913  LC6 F 501  HOH F 919                               
SITE     1 AC4 14 ARG B 263  LC6 B 501  HIS D 224  ALA D 227                    
SITE     2 AC4 14 PHE D 228  MET D 250  PHE D 254  ARG D 263                    
SITE     3 AC4 14 THR D 266  LEU D 267  PHE D 270  GLY D 271                    
SITE     4 AC4 14 ILE D 294  HIS E 320                                          
SITE     1 AC5 15 GLU C 225  THR C 226  HIS E 224  THR E 226                    
SITE     2 AC5 15 ALA E 227  GLY E 230  LYS E 234  LEU E 235                    
SITE     3 AC5 15 MET E 250  ARG E 263  THR E 266  LEU E 267                    
SITE     4 AC5 15 PHE E 270  SER F 255  ARG F 300                               
SITE     1 AC6 13 HIS A 320  VAL C 258  ARG C 263  LC6 C 501                    
SITE     2 AC6 13 ALA F 227  LEU F 235  MET F 250  PHE F 254                    
SITE     3 AC6 13 ARG F 263  THR F 266  LEU F 267  PHE F 270                    
SITE     4 AC6 13 GLY F 271                                                     
CRYST1   37.288   65.498   97.773 101.92  89.83  99.26 P 1           6          
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      0.026818  0.004371  0.000849        0.00000                         
SCALE2      0.000000  0.015469  0.003302        0.00000                         
SCALE3      0.000000  0.000000  0.010458        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system